Isoenzymes (or isozymes) are a group of enzymes that catalyze the same reaction but have different enzyme forms and catalytic efficiencies. Isozymes are usually distinguished by their electrophoretic mobilities.
The normal serum protein level is 6.3-8.3 g/dL. The main proteins in serum are albumin, globulins, fibrinogen, and prothrombin. Albumin is synthesized in the liver while globulins are synthesized in the liver, spleen, and bone marrow. The protein fractions can be measured using electrophoresis, precipitation, immuno-electrophoresis, salting out, or ultracentrifugation. Albumin is the major transport protein while globulins include antibodies and proteins like transferrin. Fibrinogen is important for blood clotting. Abnormal levels of total proteins or specific fractions can indicate various health conditions.
The major dietary lipids are triacylglycerols, cholesterol, phospholipids, and free fatty acids. Lipids are insoluble in water and require digestion by lipases and emulsification by bile salts to be broken down into absorbable components. In the small intestine, pancreatic lipase breaks triacylglycerols into fatty acids and monoacylglycerols within mixed micelles. Bile salts also aid in emulsifying lipids into smaller particles. Digestion products are absorbed via micelle diffusion and resynthesized into triglycerides and phospholipids within intestinal cells before transport to the liver via the lymphatic system or blood.
This document discusses cholesterol, including its structure, properties, sources, and importance. Cholesterol has the molecular formula C27H45OH and possesses a cyclopentano perhydro phenanthrene nucleus. It is synthesized endogenously in the body and obtained exogenously through diet. Cholesterol is an important component of cell membranes and is a precursor for bile acids, steroid hormones like estrogen and testosterone, and vitamin D3. It occurs both in free and esterified forms in the body and liver plays a key role in regulating cholesterol levels.
This document discusses various clinical enzymology topics including enzymes, isoenzymes, classification of enzymes, diagnostic uses of enzymes, and specific enzymes elevated in certain diseases. It provides information on enzymes that can help diagnose acute myocardial infarction (CK, AST, LDH), liver diseases (aminotransferases, GGT), bone diseases (alkaline phosphatase, acid phosphatase), and GI tract diseases (amylase, lipase). The levels and timing of elevation of these enzymes in different conditions is outlined.
Proteins are the macromolecules responsible for the biological processes in the cell. They consist at their most basic level of a chain of amino acids, determined by the sequence of nucleotides in a gene. Depending on the amino acid sequence (different amino acids have different biochemical properties) and interactions with their environment, proteins fold into a three-dimensional structure, which allows them to interact with other proteins and molecules and perform their function
The TCA cycle, also known as the Krebs cycle or citric acid cycle, is the central metabolic pathway that catalyzes the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins to produce carbon dioxide, water, and energy in the form of ATP, NADH, and FADH2. The TCA cycle occurs in the mitochondrial matrix and is the final common pathway for the oxidation of these three macronutrient types. Through a series of chemical reactions, acetyl-CoA is oxidized, producing carbon dioxide and hydrogen ions that will be used in the electron transport chain to generate ATP through oxidative phosphorylation.
The multiple forms of an enzyme catalyzing the same chemical reaction are called isoenzmyes. They, however, differ in their physical and chemical properties.
Examples: Isozymes of numerous dehydrogenases, and several oxidases, transaminases, phosphatases, transphosphorylases, proteolytic enzymes, aldolases.
This document discusses the use of enzymes as diagnostic tools in clinical chemistry. It provides examples of various enzymes found in different tissues that can be measured in blood and other samples to detect abnormalities and diseases. When concentrations of enzymes are outside normal ranges it can indicate tissue damage or metabolic issues. The document outlines several enzymes and their clinical significance, such as using lactate dehydrogenase to detect heart attacks or alanine transaminase to detect liver damage. It also discusses using isoenzyme patterns and specific assays to distinguish between tissue types when enzyme levels are elevated.
The urea cycle is a cyclic process that occurs primarily in the liver to convert toxic ammonia into urea for excretion. It involves 5 enzyme-catalyzed reactions, 3 in the mitochondria and 2 in the cytosol. The cycle uses 3 ATP and produces 1 molecule of urea while recycling ornithine. Defects in urea cycle enzymes can cause hyperammonemia, which can be toxic if ammonia levels rise and impair the tricarboxylic acid cycle in the brain. The presentation provided details on the individual reactions, regulation, energetics, disorders like hepatic coma, and inherited urea cycle defects.
Coenzyme - Introduction, Definition, Examples for coenzyme, reaction catalysed by coenzyme, Types of coenzymes - cosubstrate and prosthetic group coenzymes, second type of classification of coenzyme- hydrogen group transfer , other than hydrogen group transfer.
This document summarizes the digestion and absorption of proteins. It explains that proteins are broken down into amino acids by proteolytic enzymes in the stomach, pancreas, and small intestine. These amino acids are then absorbed into the bloodstream through active transport mechanisms in the intestinal epithelium. Genetic disorders like Hartnup's disease and cystinuria can impair amino acid transport and cause amino acids to be lost in urine or feces.
Lipoproteins are spherical complexes formed by lipids and proteins that transport insoluble lipids through the blood. There are four main classes of lipoproteins: chylomicrons, very low density lipoproteins (VLDL), low density lipoproteins (LDL), and high density lipoproteins (HDL). Chylomicrons and VLDL are involved in transporting triglycerides, LDL transports cholesterol, and HDL transports excess cholesterol from tissues back to the liver.
Enzymes are proteins that act as biological catalysts, speeding up chemical reactions in cells without being consumed. They are highly specific and can catalyze reactions like metabolism. Enzymes are composed of amino acid chains and sometimes require cofactors to function. They act by binding to substrates at active sites in a lock-and-key or induced fit mechanism. Factors like temperature, pH, concentration of enzymes and substrates affect reaction rates. Enzymes play important roles in the body like digestion, synthesis, degradation of molecules, and protection against pathogens.
Plasma enzymes can be either plasma-derived or cell-derived. Lactate dehydrogenase (LDH) and creatine phosphokinase (CPK) are examples of enzymes that exist as multiple isoenzyme forms with tissue-specific patterns. Measurement of isoenzyme levels can provide clinical information about tissue injury or disease. For example, elevated levels of specific LDH or CPK isoenzymes can indicate myocardial infarction, while others may signify muscle, liver, or cancerous diseases. Alkaline phosphatase also demonstrates isoenzyme patterns that are increased in conditions like liver obstruction or bone diseases.
Ketone bodies are produced when fatty acids are broken down in the liver. They serve as an alternative energy source for tissues when glucose is limited, such as during fasting or diabetes. Ketone bodies are synthesized in the liver through a series of reactions starting with acetyl CoA. Their production is regulated by substrate availability, fatty acid oxidation, ATP levels, and the enzyme HMG CoA synthase. Tissues such as the brain can use ketone bodies for energy through another series of reactions. Excessive ketone body production causes ketosis, characterized by ketonemia, ketonuria, and metabolic acidosis. Ketosis is managed by restoring carbohydrate metabolism and correcting electrolyte and acid-base imbalances.
Lipoproteins are biochemical compounds consisting of proteins and lipids that transport lipids like cholesterol through the bloodstream. They are classified based on density and include chylomicrons, very low density lipoproteins, low density lipoproteins, and high density lipoproteins. Lipoproteins metabolize through exogenous and endogenous pathways to transport lipids from the intestines and liver to tissues.
Lipoproteins are biochemical assemblies that transport hydrophobic lipid molecules in water and blood. They consist of a phospholipid and cholesterol outer shell with apolipoproteins embedded that stabilize the complex and determine its function. The main types of lipoproteins are chylomicrons, VLDL, IDL, LDL, and HDL, which differ in size, density, and lipid and protein composition. They enable the transport and metabolism of triglycerides, cholesterol, and other lipids throughout the body.
This document discusses acid-base disorders including acidosis and alkalosis. It defines metabolic and respiratory acidosis and alkalosis based on primary disturbances in bicarbonate or pCO2 levels. Compensatory responses between the respiratory and renal systems are described. Causes, examples, and management of respiratory acidosis and alkalosis are provided. Arterial blood gas analysis is explained as a tool to measure acid-base levels and oxygen status in patients with conditions like lung disease. One case presented is identified as chronic respiratory acidosis based on elevated pCO2 and bicarbonate levels.
This document discusses essential fatty acids and omega-3 and omega-6 fatty acids. It defines fatty acids and describes their nomenclature and types. Essential fatty acids cannot be synthesized in the human body and must come from diet, including omega-3 and omega-6 polyunsaturated fatty acids. These are important for cell membrane formation, brain and nervous system function, and producing hormone-like substances. The document outlines food sources of omega-3 and omega-6 fatty acids and provides an example structure and synthesis pathway. It discusses the clinical significance of omega-6 in inflammation and eicosanoid production, and some potential benefits of omega-6 fatty acids.
Lactate dehydrogenase (LDH) is an enzyme that catalyzes the conversion of lactate to pyruvate. It exists as five isoenzymes (LDH-1 to LDH-5) that differ in their subunit composition and electric charge. The isoenzymes show varying tissue distribution, catalytic properties, and clinical significance. Elevated levels of specific isoenzymes can help identify the origin of tissue damage, as LDH-1 and LDH-2 indicate myocardial infarction while LDH-4 and LDH-5 signify liver damage. The LDH isoenzyme pattern also provides information about different cancer types.
ISOENZYME
INTRODUCTION
HISTORY
DEFINATION
EXPLANATION FOR THE EXISTENCE OF ISOENZYME
IMPORTANT EXAMPLE OF ISOENZYME
LACTATE DEHYDROGENASE(LDH)
CREATINE PHOSPHOKINASE(CPK)
ALKALINE PHOSPHATASE (ALP)
REFERENCE
Isoenzymes are multiple forms of the same enzyme that catalyze the same reaction but differ in their primary structure and kinetic properties. Isoenzymes can exist due to different genes producing the same enzyme, oligomeric enzymes consisting of different subunit types, differences in whether the enzyme is active as a monomer or oligomer, or differences in carbohydrate content for glycoprotein enzymes. Examples of enzymes with important isoenzymes include lactate dehydrogenase, creatine kinase, and alkaline phosphatase. Isoenzymes allow for the diagnosis of diseases by their changing levels and subtypes in conditions affecting tissues like heart, liver, and cancer.
Metabolism involves the breakdown (catabolism) and building (anabolism) of molecules in the body. Enzymes are proteins that catalyze metabolic reactions and are made up of amino acids folded into shapes with active sites. Enzymes require cofactors like vitamins and minerals to function as holoenzymes in reactions. Enzyme activity is affected by factors like temperature, substrate concentration, and pH - with each enzyme having optimal conditions for maximum reaction rates.
An enzyme is a biological catalyst and is almost always a protein. It speeds up the rate of a specific chemical reaction in the cell. The enzyme is not destroyed during the reaction and is used over and over.
1. The document discusses the structure, properties, and mechanisms of enzyme action.
2. It describes how enzymes are classified and named based on their reactions.
3. Key factors that affect enzyme activity like pH, temperature, inhibitors, and cofactors are explained.
1) The document discusses lipid metabolism, focusing on cholesterol and lipoproteins. It covers the structure, biosynthesis, regulation, and excretion of cholesterol.
2) Lipoproteins are classified based on their density, and include chylomicrons, VLDL, IDL, LDL, and HDL. Chylomicrons transport dietary lipids from the intestine to tissues, while VLDL transports endogenous lipids from the liver.
3) Chylomicrons and VLDL are broken down by lipoprotein lipase in tissues, generating fatty acids. Their remnants are taken up by the liver via receptor-mediated endocytosis.
his video explains the different Characteristics of enzymes like specificity, efficiency, catalytic, protein and colloidal nature.
https://youtu.be/EzCSWQAv7so link for you tube video
This document defines enzymes and describes their key characteristics. It states that enzymes are biological catalysts that speed up chemical reactions without being used up in the process. The document outlines several models of enzyme action, including the lock-and-key and induced fit models. It also discusses factors that can affect an enzyme's activity, such as substrate concentration, temperature, and pH. Finally, it describes how enzymes are classified and their high specificity for particular reactions and substrates.
Enzymes are protein catalysts that speed up biochemical reactions without being consumed. They are found in living cells and are usually highly specific. The document categorizes enzymes into six major classes based on the type of reaction they catalyze. It also discusses factors that affect enzyme activity such as pH, temperature, and substrate/enzyme concentration. Diagnostic enzymes are discussed that can provide information about the health of specific organs.
Enzymes are protein catalysts that accelerate biochemical reactions without being consumed. They are produced by living cells and work by lowering the activation energy of reactions. Enzymes are classified based on the type of reaction they catalyze, such as oxidoreductases that catalyze redox reactions or hydrolases that catalyze hydrolysis reactions. The enzyme binds to its substrate at the active site in a lock-and-key or induced fit mechanism to form an enzyme-substrate complex that is converted to products and releases the recycled enzyme. Enzymes have an optimal pH and temperature range for activity and are essential for all cellular functions like metabolism, cell signaling, and DNA replication.
This document provides information about enzymes. Some key points:
- Enzymes are protein catalysts that speed up chemical reactions without being consumed. They have specific active sites that substrates bind to in order to undergo reactions.
- There are six major classes of enzymes based on the type of reaction they catalyze: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases.
- Enzymes exhibit specificity in terms of the substrates, reactions, and stereoisomers they act on. Their active sites allow for selective binding.
- In addition to the protein component, some enzymes require cofactors like metals ions or coenzymes to function properly
This document summarizes lipoprotein metabolism. It discusses that lipoproteins are spherical particles composed of lipids and proteins that transport relatively insoluble lipids through the aqueous blood. It describes the different types of lipoproteins, including their compositions, sizes, densities, and roles in transporting lipids such as triglycerides and cholesterol. In particular, it focuses on very low density lipoproteins (VLDL), detailing their production and metabolism, through the actions of lipoprotein lipase and other proteins, into intermediate and low density lipoproteins which transport cholesterol. It also discusses related clinical conditions like hyperlipoproteinemias.
This document discusses enzymes, including their structure, classification, and mechanisms of action. It defines enzymes as proteins that lower the activation energy of chemical reactions and notes they are not consumed during reactions. It describes important enzyme components like active sites and cofactors/coenzymes. It explains environmental factors and inhibitors that can affect enzyme activity. Different classification systems are presented, and key terms like substrate specificity and enzyme naming conventions are outlined.
5. Biochemistry of enzymes edited 2024.pptxmohammed959032
Enzymes are biological catalysts that regulate biochemical reactions. This document discusses the composition, mechanisms, and factors that influence enzyme activity. It describes how enzymes lower activation energy and use an active site to bind substrates and stabilize reaction intermediates. The Michaelis-Menten equation models how reaction rate varies with substrate concentration in relation to parameters like Vmax and Km. Environmental factors like temperature and pH can impact enzyme activity.
1. Enzymes are protein catalysts that accelerate biochemical reactions in living cells.
2. They are classified based on the type of reaction they catalyze such as oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases.
3. Enzyme activity is affected by factors like pH, temperature, and inhibitors. Competitive and non-competitive inhibitors bind at the active site or other regions respectively.
- Enzymes are protein biocatalysts that increase the rate of chemical reactions without being consumed. They are specific in their action and composed of apoenzyme and coenzyme.
- The active site of an enzyme binds specifically to substrates and contains residues that help hold the substrate. Changes to the active site shape affect enzyme function.
- Factors like temperature, pH, substrate/product concentration, and presence of activators or inhibitors can regulate an enzyme's activity rate. Studying an enzyme's kinetics reveals its catalytic mechanism.
- Regulation allows cells to control metabolic pathways by modulating enzyme activity. Competitive inhibitors bind the active site while non-competitive inhibitors cause conformational changes. I
Group Dynamic(presentation for nursing management)ABHIJIT BHOYAR
Group dynamics is a system of behaviors and psychological processes occurring within a social group (intragroup dynamics), or between social groups (intergroup dynamics)
the practice of training people to obey rules and behave well.
the practice of training your mind and body so that you control your actions and obey rules; a way of doing this
1. Enzymes like ALT, AST, ALP, GGT, CK, troponins, and PSA are used as biomarkers to diagnose diseases of the liver, heart, bones, muscles, and prostate.
2. Elevated levels of the liver enzymes ALT, AST, ALP, and GGT indicate potential liver damage or disease.
3. CK and troponin levels are measured to diagnose heart attacks, while high PSA levels may indicate prostate cancer.
A complete cholesterol test — also called a lipid panel or lipid profile — is a blood test that can measure the amount of cholesterol and triglycerides in your blood
Cholesterol is a waxy substance found in your blood. Your body needs cholesterol to build healthy cells, but high levels of cholesterol can increase your risk of heart disease.
Lipid metabolism entails the oxidation of fatty acids to either generate energy or synthesize new lipids from smaller constituent molecules. Lipid metabolism is associated with carbohydrate metabolism,
LIPIDS-Digestion and absorption of Lipids.pptxABHIJIT BHOYAR
The digestion of lipids begins in the oral cavity through exposure to lingual lipases, which are secreted by glands in the tongue to begin the process of digesting triglycerides.
The term essential fatty acids (EFA) refers to those polyunsaturated fatty acids (PUFA) that must be provided by foods because these cannot be synthesized in the body yet are necessary for health
Fatty acids are the building blocks of the fat in our bodies and in the food we eat. During digestion, the body breaks down fats into fatty acids, which can then be absorbed into the blood. Fatty acid molecules are usually joined together in groups of three, forming a molecule called a triglyceride.
The document defines lipids and classifies them. It discusses that lipids are a diverse group of organic compounds that are hydrophobic and insoluble in water. Lipids serve important functions like energy storage, cellular structure, signaling and energy transport. Lipids are classified as simple lipids, complex lipids, derived lipids and miscellaneous lipids. Simple lipids include fats, oils and waxes. Complex lipids contain additional groups like phosphate, carbohydrates or proteins. The document provides examples and descriptions of different lipid classes.
Once the egg has left the ovary it can be fertilized and implant itself in the lining of the uterus. The main function of the uterus is to nourish the developing fetus prior to birth.
he kidneys are a vital organ critical to the human body. From filtering waste from blood to produce red blood cells, it serves a crucial role. With cells and tissue that work together in synchronized form for common function
The liver is the largest solid organ located in the upper right abdomen. It performs hundreds of vital functions including removing toxins from the blood, maintaining blood sugar levels, and regulating blood clotting. The liver receives 20% of its blood supply from the hepatic artery and 80% from the portal vein. It is divided into four lobes and has five surfaces. The liver plays a crucial role in metabolism and detoxification.
If you like share this PPT presentation to nursing students. The pancreas is an organ and a gland. Glands are organs that produce and release substances in the body. The pancreas performs two main functions: Exocrine function: Produces substances (enzymes) that help with digestion.
he spleen is a fist-sized organ found in the upper left side of your abdomen, next to your stomach and behind your left ribs. It's an important part of your immune system but you can survive without it. This is because the liver can take over many of the spleen's functions
The Popliteal Fossa is a diamond-shaped space behind the knee joint. It is formed between the muscles in the posterior compartments of the thigh and leg. This anatomical landmark is the major route by which structures pass between the thigh and leg.
The femoral triangle is an anatomical region in the upper thigh bounded laterally by the sartorius muscle and medially by the adductor longus muscle. Its base is formed by the inguinal ligament and its apex points downwards. The femoral triangle contains the femoral artery and vein, branches of the femoral nerve, and deep inguinal lymph nodes. The femoral sheath encloses the upper part of the femoral vessels and is divided into three compartments. The contents of the femoral triangle are clinically relevant to femoral hernias, nerve injuries, and vascular procedures.
This topic is related to the joints.
it is a type of synovial joint.
it is a ball and socket type.
This is very sensative joint and easy to have fracture to this part.
How can we use AI to give healthcare providers and administrators superpowers in serving their patients and communities? We are bombarded with breathless enthusiasm and often feel we are missing out or are ignorant where others are wise. After this session, you should be able to address:
• What is current practice and sentiment within leading edge healthcare organizations?
• How should we select use cases?
• What are the most common necessities left off the AI checklist?
• What tools, processes, and types of people do you need in place to scale?
The link between skin conditions and mental health issues can be common; problems like dermatitis, acne, and psoriasis often connect with psychological factors. Mind care is crucial for addressing these skin disorders effectively and improving overall well-being.
TEST BANK For Auditing & Assurance Services ASystematic Approach, 12th Editio...rightmanforbloodline
TEST BANK For Auditing & Assurance Services ASystematic Approach, 12th EditionChapters 1 - 21 Complete.pdf
TEST BANK For Auditing & Assurance Services ASystematic Approach, 12th EditionChapters 1 - 21 Complete.pdf
The Future of Ophthalmology: Dr. David Greene's Stem Cell Vision RestorationDr. David Greene Arizona
The future of ophthalmology is bright, thanks in large part to the pioneering work of Dr. David Greene. His advancements in stem cell therapy offer a beacon of hope for those suffering from vision loss. As research progresses, we can look forward to a world where restoring sight is not just a possibility, but a reality.
Statistics from Finland, provided by the Contact Point for Cross-Border Health Care in Finland and Kela (the Social Insurance Institution of Finland) include information on cross-border healthcare, European Health Insurance Card (EHIC), medical care costs incured abroad and their reimbursements, and prior authorisations for seeking treatment abroad.
When Decision-Making Is Imperative: Advance Care Planning for Busy Practice S...VITASAuthor
Complex, chronically ill patients present an opportunity to discuss and implement hospice and palliative care. Many elderly patients who present to the ED and other busy practice settings are hospice-eligible because of functional decline and multi-morbidity. Key tools can quickly facilitate goals-of-care (GOC) conversations, advance care planning, and hospice referrals amid time constraints and high-acuity challenges.
Must-Have Baby Products for New Parents.pdfCuddables
Are you looking for safe & secure baby wipes, Cuddables is here for you. Our wipes are dermatologist approved which makes it no.1 choice of parents. Get rid of unexpected spit-ups and spill-ups anytime. Order now and get buy 1 and get 1 free.-https://www.cuddables.in/products/baby-wipes
PRESCRIBING II - FUNDAMENTALS OF PRESCRIBING MODULE Part II.pptxWifem1
As per INC revised syllabus IV semester students are having prescription module. Its related to that prescription module. IV semester student will be benefited by this. This ppt deals about basic information of prescription module why we need to study, why the nurses in need of writing prescription
Benefits:
Stress Relief
Relaxation and rejuvenation of the mind. Stabilizing the nervous system
Maintaining mental clarity and relaxation
Achieving spiritual peace and mental growth.
From the age of about thirteen girls have their periods and they get pain in the lower abdomen. Performing this mudra only for 5-10 minutes relieves the pain.
Scanty or excess bleeding will be regulated.
Practicing this mudra every day for 10 minutes followed by prana mudra will solve the menopause related problems.
UNIVERSAL IMMUNIZATION PROGRAMME BY ANUSHRI.pptxAnushriSrivastav
Immunization Programme is the one of the largest programme of world. This programme in India was introduced by WHO in 1978 as Expanded Programme of Immunization (EPI).
In 1985 it was expanded as Universal Immunization Programme that covers all the districts in country by 1989-90 .UIP become a part of CSSM in 1992 and RCH in 1997 and is currently one of the key areas under NRHM since 2005
The action of making a person or animal resistant to a particular infectious disease or pathogens typically by vaccination .
Or
According to WHO – Immunization is the process whereby a person is made immune or resistant to an infectious disease ,typically by the administration of a vaccine
1978: Expanded Programme of immunization (EPI).
Limited reach - mostly urban
1985: Universal Immunization Programme (UIP).
For reduction of mortality and morbidity due to 6 VPD’s.
Indigenous vaccine production capacity enhanced
Cold chain established
Phased implementation - all districts covered by 1989-90.
Monitoring and evaluation system implemented
1986: Technology Mission On Immunization
Monitoring under PMO’s 20 point programme
Coverage in infants (0 – 12 months) monitored
1992: Child Survival and Safe Motherhood (CSSM)
Included both UIP and Safe motherhood program
1997: Reproductive Child Health (RCH 1)
2005: National Rural Health Mission (NRHM)
2012: Government of India declared 2012 as “Year of Intensification of Routine Immunization.
2013: India, along with other South-East Asia Region, declared commitment towards measles elimination and rubella/congenital rubella syndrome (CRS) control by 2020.
2014: No Wild Polio virus case was reported from the country for the last three years and India had a historic achievement and was certified as “polio free country” along with other South East Asia Region (SEAR) countries of WHO.
To reduce morbidity and mortality of the major six childhood disease .
To achieve 100% coverage for eligible children.
To develop a surveillance system .
To minimize the efforts and cost of treatment.
To deliver an integrated immunization services through health centres .
To promote a new healthy generation .
Training of all health personnel .
Strengthening the cold chain .
Promotion of community participation .
Integrate vaccination session with PHC services .
Ensuring regular supply of potent vaccine
Under five year children .
Women in the child bearing age (15-45years).
Schedule of immunization .
Types of the vaccine .
Dose of each vaccines .
Route of administration.
Precautions of vaccinations .
RI targets to vaccinate 27 million new born each year with all primary doses and ~100 million children of 1-5 year age with booster doses of UIP vaccines. In addition, 30 million pregnant mothers are targeted for TT vaccination each year. To vaccinate this cohort of 157 million beneficiaries, ~10 million immunization sessions are conducted, majority of these are at village level
Strategy and policy
2. Specific Learning Objectives
At the end of the lecture, student should be able to:
1. Define isoenzymes
2. Explain properties of isoenzyme
3. Introduction
• The multiple forms of an enzyme catalysing the same
reaction are isoenzymes or isozymes. They, however,
differ in their physical and chemical properties which
include the structure, electrophoretic and
immunological properties, K m and V max values, pH
optimum, relative susceptibility to inhibitors and degree
of denaturation.
5. • In biochemistry, isozymes are enzymes that differ in
amino acid sequence but catalyze the same chemical
reaction.
• Isozymes usually have different kinetic parameters, or
are regulated differently. They permit the fine-tuning of
metabolism to meet the particular needs of a given
tissue or developmental stage.
9. Explanation for the existence of isoenzymes
• Many possible reasons are offered to explain the
presence of isoenzymes in the living systems.
• 1. Isoenzymes synthesized from different genes e.g.
malate dehydrogenase of cytosol is different from that
found in mitochondria.
• 2. Oligomeric enzymes consisting of more than one
type of subunits e.g. lactate dehydrogenase and
creatine phosphokinase.
10. Cont..
• 3. An enzyme may be active as monomer or oligomer
e.g. glutamate dehydrogenase.
• 4. In glycoprotein enzymes, differences in carbohydrate
content may be responsible for isoenzymes e.g.
alkaline phosphatase.
11. Isoenzymes of lactate dehydrogenase (LDH)
• LDH whose systematic name is L-lactateNAD+
oxidoreductase (E.C. 1.1.1.27) catalyses the
interconversion of lactate and pyruvate
12. Structure of LDH isoenzymes :
• LDH is an oligomeric (tetrameric) enzyme made up of
four polypeptide subunits.
• Two types of subunits namely M (for muscle) and H (for
heart) are produced by different genes.
• M–subunit is basic while H subunit is acidic.
• The isoenzymes contain either one or both the
subunits giving LDH1 to LDH5.
13. Significance of differential catalytic activity :
LDH1 (H4)
• LDH1 (H4) is predominantly found in heart muscle and
is inhibited by pyruvate – the substrate. Hence,
pyruvate is not converted to lactate in cardiac muscle
but is converted to acetyl CoA which enters citric acid
cycle.
• LDH5 (M4) is mostly present in skeletal muscle and the
inhibition of this enzyme by pyruvate is minimal,hence
pyruvate is converted to lactate. Further,LDH5 has low
Km (high affinity) while LDH1 has high Km (low affinity)
for pyruvate.
14. • The differential catalytic activities of LDH1 and LDH5 in
heart and skeletal muscle, respectively, are well suited
for the aerobic (presence of oxygen) and anaerobic
(absence of oxygen) conditions, prevailing in these
tissues.
15. Diagnostic importance of LDH :
• Isoenzymes of LDH have immense value in the
diagnosis of heart and liver related disorders
• In healthy individuals, the activity of LDH2 is higher
than that of LDH1 in serum.
• In the case of myocardial infarction, LDH1 is much
greater than LDH2 and this happens within 12 to
24 hours after infarction. Increased activity of LDH
16. Isoenzymes of creatine phosphokinase
Creatine kinase (CK) or creatine phosphokinase
(CPK) catalyses the inter-conversion of
phosphocreatine (or creatine phosphate) to creat
17. Isoenzymes of alkaline phosphatase
• As many as six isoenzymes of alkaline
phosphatase (ALP) have been identified.
• ALP is a monomer, the isoenzymes are due to
the difference in the carbohydrate content (sialic
acid residues).
• The most important ALP isoenzymes are D1-
ALP, D2-heat labile ALP, D2-heat stable ALP,
pre-E ALP, J-ALP etc
18. Isoenzymes of alcohol dehydrogenase
• Alcohol dehydrogenase (ADH) has two
heterodimer isoenzymes.
• Among the white Americans and Europeans, DE1
isoenzyme is predominant whereas in Japanese
and Chinese (Orientals) DE2 is mostly present.
• The isomer DE2 more rapidly converts alcohol to
acetaldehyde.
19. Properties of isoenzymes
1. Electrophoretic- E.g Isoenzymes of Lactate
dehydrogenase have mobility different electrophoretic
mobility
2. Heat stability-E.g Alkaline phosphatase isoenzymes
are either heat labile or stable
3. Inhibitor- E.g An inhibitor can inhibit only one
isoenzyme of an enzyme eg. Acid phosphatase
20. Cont..
4. Cofactors Mitochondrial isocitrate dehydrogenase
requires NAD+ , cytosolic form requires NADP+
5. Tissue localization-Eg LDH 1 is present in heart,
LDH 5 in muscle
6. Antibodies-For creatine kinase, each isoenzyme can
be bound only by a specific antibody 3
21. Expsected Question
• Essay / Situational Question
• Describe isoenzymes with reference to definition and
properties , chemical nature and factors affecting
isoenzyme activity
• Short Question
1. Explain characteristic of isoenzyme
2. Describe Classification of isoenzyme
3. Describe factors influencing isoenzyme activity