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Questions and Answers
Which isoenzyme of aminotransferases is primarily derived from platelets, erythrocytes, and monocytes?
Which isoenzyme of aminotransferases is primarily derived from platelets, erythrocytes, and monocytes?
- Band 5 Isoenzyme
- Band 2 Isoenzyme
- Band 3 Isoenzyme (correct)
- Alanine Aminotransferase
What is the cofactor required for the activity of alanine aminotransferase?
What is the cofactor required for the activity of alanine aminotransferase?
- Thiamine
- NAD+
- Folate
- Pyridoxal-5'-phosphate (correct)
What is the primary function of aspartate aminotransferase?
What is the primary function of aspartate aminotransferase?
- Transfer of an amino group between aspartate and α-ketoacids (correct)
- Breakdown of fatty acids
- Synthesis of nucleotide precursors
- Conversion of glutamate to proline
Which isoenzyme is mentioned as being resistant to tartrate inhibition?
Which isoenzyme is mentioned as being resistant to tartrate inhibition?
In which condition is positive ACP evident in a vaginal swab within the first 12 hours up to four days?
In which condition is positive ACP evident in a vaginal swab within the first 12 hours up to four days?
What is the ideal pH range for most physiological reactions to occur?
What is the ideal pH range for most physiological reactions to occur?
Which temperature is recommended for the storage of substrates and coenzymes?
Which temperature is recommended for the storage of substrates and coenzymes?
What type of enzyme inhibitor competes with the substrate for the active site?
What type of enzyme inhibitor competes with the substrate for the active site?
What is a disadvantage of measuring enzyme activity at the end of the reaction?
What is a disadvantage of measuring enzyme activity at the end of the reaction?
In multi-point assays, how is the concentration of the indicator substance measured?
In multi-point assays, how is the concentration of the indicator substance measured?
Which of the following best describes uncompetitive inhibition?
Which of the following best describes uncompetitive inhibition?
What is the unit commonly used for expressing enzymatic activity?
What is the unit commonly used for expressing enzymatic activity?
What effect does hemolysis have on enzyme concentration measurements?
What effect does hemolysis have on enzyme concentration measurements?
What is the primary physiological role of Alkaline Phosphatase (ALP)?
What is the primary physiological role of Alkaline Phosphatase (ALP)?
Which condition is NOT associated with elevated levels of ALP?
Which condition is NOT associated with elevated levels of ALP?
Regan ALP, a variant of alkaline phosphatase, is primarily found in which type of cancers?
Regan ALP, a variant of alkaline phosphatase, is primarily found in which type of cancers?
Decreased serum levels of ALP are indicative of which condition?
Decreased serum levels of ALP are indicative of which condition?
Which ALP variant is specifically associated with adenocarcinoma of the pancreas?
Which ALP variant is specifically associated with adenocarcinoma of the pancreas?
Which of the following substances is known to inhibit Regan ALP?
Which of the following substances is known to inhibit Regan ALP?
The most heat-stable variant of ALP is which type?
The most heat-stable variant of ALP is which type?
What are common conditions that can lead to elevated levels of ALP?
What are common conditions that can lead to elevated levels of ALP?
Which tissue is a major source of mitochondrial AST?
Which tissue is a major source of mitochondrial AST?
In which condition would you expect an increase in both AST and ALT levels?
In which condition would you expect an increase in both AST and ALT levels?
What is a reference range for AST levels?
What is a reference range for AST levels?
Which of the following conditions can lead to decreased AST levels?
Which of the following conditions can lead to decreased AST levels?
What is the role of creatine kinase (CK) in muscle metabolism?
What is the role of creatine kinase (CK) in muscle metabolism?
During periods of active muscle contraction, what happens to creatine phosphate?
During periods of active muscle contraction, what happens to creatine phosphate?
Which enzyme is specifically noted for being a bone isoenzyme?
Which enzyme is specifically noted for being a bone isoenzyme?
What typically causes an increase in AST levels by 4-10 times the upper limit of normal?
What typically causes an increase in AST levels by 4-10 times the upper limit of normal?
What enzyme is primarily associated with the conversion of angiotensin I to angiotensin II?
What enzyme is primarily associated with the conversion of angiotensin I to angiotensin II?
Which enzyme is rarely used but considered an excellent marker for liver disease?
Which enzyme is rarely used but considered an excellent marker for liver disease?
What typically leads to an elevation of Angiotensin-Converting Enzyme levels?
What typically leads to an elevation of Angiotensin-Converting Enzyme levels?
What is the most common reason for testing pseudocholinesterase activity?
What is the most common reason for testing pseudocholinesterase activity?
In which organ is pseudocholinesterase predominantly found?
In which organ is pseudocholinesterase predominantly found?
What structural characteristic is associated with cholinesterase?
What structural characteristic is associated with cholinesterase?
Which condition is associated with low activity of cholinesterase enzymes?
Which condition is associated with low activity of cholinesterase enzymes?
What happens to the activity of Angiotensin-Converting Enzyme as fibrosis progresses?
What happens to the activity of Angiotensin-Converting Enzyme as fibrosis progresses?
What is the primary function of Gamma-Glutamyl Transferase (GGT)?
What is the primary function of Gamma-Glutamyl Transferase (GGT)?
Which condition is GGT considered a very sensitive indicator for?
Which condition is GGT considered a very sensitive indicator for?
In which tissue does GGT predominantly reside as plasma membrane bound?
In which tissue does GGT predominantly reside as plasma membrane bound?
What is the typical half-life of GGT in healthy individuals?
What is the typical half-life of GGT in healthy individuals?
Which of the following conditions is NOT associated with elevated GGT levels?
Which of the following conditions is NOT associated with elevated GGT levels?
What effect does smoking have on GGT levels?
What effect does smoking have on GGT levels?
Which of the following is the reference value range for GGT in males?
Which of the following is the reference value range for GGT in males?
Which of the following diseases would most likely lead to the highest elevation of total CK levels?
Which of the following diseases would most likely lead to the highest elevation of total CK levels?
Flashcards
Zero Order Reaction
Zero Order Reaction
A reaction whose rate is constant and independent of substrate concentration, but directly proportional to enzyme concentration
Competitive Inhibitor
Competitive Inhibitor
A substance that competes with the substrate for the enzyme's active site, leading to reversible inhibition.
Non-competitive Inhibitor
Non-competitive Inhibitor
A substance that inhibits an enzyme by binding to a site other than the active site (allosteric site).
Multi-point Assay
Multi-point Assay
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Uncompetitive Inhibitor
Uncompetitive Inhibitor
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Kinetic Assay
Kinetic Assay
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Coupled Reactions
Coupled Reactions
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International Unit (I.U.)
International Unit (I.U.)
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Alkaline Phosphatase (ALP)
Alkaline Phosphatase (ALP)
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ALP Function
ALP Function
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Elevated ALP Causes
Elevated ALP Causes
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ALP Reference Value
ALP Reference Value
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Increased ALP Clinical Significance
Increased ALP Clinical Significance
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Regan ALP
Regan ALP
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Nagao ALP
Nagao ALP
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Decreased ALP Clinical Significance
Decreased ALP Clinical Significance
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What are isoenzymes?
What are isoenzymes?
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What is Aspartate Aminotransferase (AST)?
What is Aspartate Aminotransferase (AST)?
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What does ACP stand for?
What does ACP stand for?
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Which isoenzyme of ACP is used for diagnosis?
Which isoenzyme of ACP is used for diagnosis?
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What does ACP's presence in vaginal swabs indicate?
What does ACP's presence in vaginal swabs indicate?
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Mitochondrial AST
Mitochondrial AST
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Tartrate-resistant ACP
Tartrate-resistant ACP
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Increased AST Levels
Increased AST Levels
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Myocardial Infarction (MI)
Myocardial Infarction (MI)
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Creatine Kinase (CK)
Creatine Kinase (CK)
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CK During Muscle Contraction
CK During Muscle Contraction
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CK During Rest
CK During Rest
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ALT (Alanine Aminotransferase)
ALT (Alanine Aminotransferase)
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GGT
GGT
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GGT and Liver Damage
GGT and Liver Damage
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GGT as Alcoholism Indicator
GGT as Alcoholism Indicator
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CK-MB and Heart Attack
CK-MB and Heart Attack
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CK-MB vs. Angina
CK-MB vs. Angina
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Duchenne Muscular Dystrophy
Duchenne Muscular Dystrophy
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GGT Reference Values
GGT Reference Values
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Smoking and GGT Levels
Smoking and GGT Levels
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Post-Hepatic Jaundice
Post-Hepatic Jaundice
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Intrahepatic Cholestasis
Intrahepatic Cholestasis
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Angiotensin-Converting Enzyme (ACE)
Angiotensin-Converting Enzyme (ACE)
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ACE Activity in Sarcoidosis
ACE Activity in Sarcoidosis
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Cholinesterase and Pseudocholinesterase
Cholinesterase and Pseudocholinesterase
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Pseudocholinesterase Deficiency
Pseudocholinesterase Deficiency
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Ornithine Carbamoyl Transferase (OCT)
Ornithine Carbamoyl Transferase (OCT)
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Activity of Liver Enzymes
Activity of Liver Enzymes
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Study Notes
Enzymes
- Specific biologic proteins catalyze biochemical reactions without altering the equilibrium point.
- Appear in serum after cellular injury, degradation of cells, or storage areas.
- High amounts of enzymes in serum indicate organ damage.
Terms Associated with Enzymes
- Holoenzyme: Active substance formed by a coenzyme (cofactor) and apoenzyme.
- Apoenzyme: Protein portion of an enzyme; subject to denaturation, losing activity if cofactor is removed.
- Isoenzyme: Different forms of the same enzyme with the same catalytic function in the body.
- Metalloenzyme: Enzyme with metal ions intrinsically part of the molecule (e.g., catalase, cytochrome oxidase).
- Proenzyme: Inactive precursor of enzymes, also called zymogens.
- Substrates: Substances acted upon by the enzyme; specific to each enzyme.
- Cofactors: Non-protein substances needed for enzyme activity (e.g., thermostable and dialyzable). Enzymes require these before manifesting enzymatic activity.
Enzyme Nomenclature
- Practical/Trivial Name: Based on the substrate name with the suffix "ase" (e.g., lipase for lipids, protease for proteins).
- Systematic Name: Based on the numerical designation given by the Enzyme Commission (EC).
- Examples: EC 1.1.1.7 for lactate dehydrogenase; EC 3.2.1.1 for amylase.
Enzyme Kinetics
- Enzyme–Substrate Interaction: An enzyme binds to a substrate to form an enzyme-substrate complex (ES). The complex can dissociate back to enzyme (E) and substrate (S). Alternatively, the complex breaks down to product (P) and free enzyme (E) if the product has a low affinity for the enzyme.
- Types of Specificity:
- Absolute Specificity: Enzymes combine with only one substrate.
- Group Specificity: Enzymes combine with all substrates containing a particular group.
- Bond Specificity: Enzymes combine with specific chemical bonds.
- Stereoisomeric Specificity: Enzymes combine primarily with one optical isomer.
Factors Affecting Enzyme Reactions
- Enzyme Concentration: Increased enzyme concentration yields increased reaction rate.
- Substrate Concentration: Increased substrate concentration increases reaction rate up to a maximum rate.
- Temperature: Reaction rate increases with temperature, approximately doubling for every 10°C rise.
- pH: Optimum pH exists for each enzyme; deviation from the optimum slows reactions.
Types of Reaction Order
- Zero-Order Reaction: Reaction rate is independent of substrate concentration and directly proportional to enzyme concentration.
General Classification of Enzymes
- Oxidoreductases: Catalyze redox (reduction-oxidation) reactions (removal or addition of electrons).
- Transferases: Catalyze the transfer of a chemical group from one substrate to another.
- Hydrolases: Catalyze hydrolysis reactions (the splitting of a bond by the addition of water).
- Lyases: Remove groups from substrates without hydrolysis, creating double bonds.
- Isomerases: Catalyze intramolecular rearrangements of substrates.
- Ligases (Synthetases): Join two substrate molecules together using energy from a high-energy phosphate.
Enzyme Inhibition
- Competitive Inhibition: Inhibitor competes with the substrate for the active site.
- Non-competitive Inhibition: Inhibitor binds to the enzyme at a site other than the active site (allosteric site).
- Uncompetitive Inhibition: Inhibitor binds to the enzyme-substrate complex.
Enzyme Induction
- Enzyme induction is the ability of an enzyme to adapt to biochemical systems.
Clinical Enzymology (Additional Topics)
- Room temperature: Ideal for storing LDH (LD4 and LD5).
- Hemolysis: Increase of enzyme concentration.
- Lactescence/milky specimens: Decrease in enzyme concentration.
- Measurement of enzyme activity: Done at the end of a reaction, usually in combination with colorimetric reaction.
- Units for expressing enzymatic activity: International Units (IU) or katal units (KU).
- Means of measuring enzyme activity: Change in coenzyme concentration; Increase in product concentration; Decrease in substrate concentration.
- Specific enzyme examples (e.g., Alkaline Phosphatase, Acid Phosphatase (ACP), Aspartate Aminotransferase (AST), Alanine Aminotransferase (ALT), Creatine Kinase (CK), Gamma-Glutamyl Transferase (GGT), Leucine Aminopeptidase (LAP), 5’ Nucleotidase (5'N), Ornithine Carbamoyl Transferase (OCT), Cholinesterase, Pseudocholinesterase, Angiotensin-Converting Enzyme (ACE), Myeloperoxidase, Aldolase, Lactate Dehydrogenase (LDH), Amylase or Diastase), their properties, and diagnostic significance.
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