6601 to 6650 MCQs for Lab Technician and Technologist Exam Preparation
5000 Plus MCQs for Lab Technician and Technologists are designed to test the knowledge and proficiency of laboratory professionals who work in the field of clinical laboratory science. These questions cover a wide range of topics related to laboratory science, including anatomy, physiology, microbiology, chemistry, and hematology.
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Questions 6601 to 6650
- Fabry’s disease is due to the deficiency of the enzyme:
- Ceramide trihexosidase ✔
- Galactocerebrosidase
- Phytanic acid oxidase
- Sphingomyelinase
- Farber’s disease is due to the deficiency of the enzyme:
- α-Galactosidase
- Ceramidase ✔
- β-Glucocerebrosidase
- Arylsulphatase A
- A synthetic nucleotide analogue, used in organ transplantation as a suppressor of immunologic rejection of grafts is
- Theophylline
- Cytarabine
- 4-Hydroxypyrazolopyrimidine
- 6-Mercaptopurine ✔
- Example of an extracellular enzyme is
- Lactate dehydrogenase
- Cytochrome oxidase
- Pancreatic lipase✔
- Hexokinase
- Enzymes, which are produced in inactive form in the living cells, are called
- Papain
- Lysozymes
- Apoenzymes
- Proenzymes ✔
- An example of ligases is
- Succinate thiokinase ✔
- Alanine racemase
- Fumarase
- Aldolase
- An example of lyases is
- Glutamine synthetase
- Fumarase ✔
- Cholinesterase
- Amylase
- Activation or inactivation of certain key regulatory enzymes is accomplished by covalent modification of the amino acid:
- Tyrosine
- Phenylalanine
- Lysine
- Serine ✔
- The enzyme which can add water to a carbon-carbon double bond or remove water to create a double bond without breaking the bond is
- Hydratase ✔
- Hydroxylase
- Hydrolase
- Esterase
- Fischer’s ‘lock and key’ model of the enzyme action implies that
- The active site is complementary in shape to that of substance only after interaction.
- The active site is complementary in shape to that of substance ✔
- Substrates change conformation prior to active site interaction
- The active site is flexible and adjusts to substrate
- A sigmoidal plot of substrate concentration ([S]) verses reaction velocity (V) may indicate
- Michaelis-Menten kinetics
- Co-operative binding ✔
- Competitive inhibition
- Non-competitive inhibition
- The Km of the enzyme giving the kinetic data as below is
- –0.50
- –0.25
- +0.25
- +0.33 ✔
- The kinetic effect of purely competitive inhibitor of an enzyme
- Increases Km without affecting Vmax ✔
- Decreases Km without affecting Vmax
- Increases Vmax without affecting Km
- Decreases Vmax without affecting Km
- If curve X in the graph (below) represents no inhibition for the reaction of the enzyme with its substrates, the curve representing the competitive inhibition, of the same reaction is
- A ✔
- B
- C
- D
- An inducer is absent in the type of enzyme:
- Allosteric enzyme
- Constitutive enzyme ✔
- Co-operative enzyme
- Isoenzymic enzyme
- A demonstrable inducer is absent in
- Allosteric enzyme
- Constitutive enzyme ✔
- Inhibited enzyme
- Co-operative enzyme
- In reversible non-competitive enzyme activity inhibition
- Vmax is increased
- Km is increased
- Km is decreased
- Concentration of active enzyme is reduced ✔
- In reversible non-competitive enzyme activity inhibition
- Inhibitor bears structural resemblance to substrate
- Inhibitor lowers the maximum velocity attainable with a given amount of enzyme ✔
- Km is increased
- Km is decreased
- In competitive enzyme activity inhibition
- The structure of inhibitor generally resembles that of the substrate ✔
- Inhibitor decreases apparent Km
- Km remains unaffective
- Inhibitor decreases Vmax without affecting Km
- In enzyme kinetics Vmax reflects
- The amount of an active enzyme ✔
- Substrate concentration
- Half the substrate concentration
- Enzyme substrate complex
- In enzyme kinetics Km implies
- The substrate concentration that gives one half Vmax ✔
- The dissocation constant for the enzyme substrate comples
- Concentration of enzyme
- Half of the substrate concentration required to achieve Vmax
- In competitive enzyme activity inhibition
- Apparent Km is decreased
- Apparent Km is increased ✔
- Vmax is increased
- Vmax is decreased
- In non competitive enzyme activity inhibition, inhibitor
- Increases Km
- Decreases Km
- Does not effect Km ✔
- Increases Km
- An enzyme catalyzing oxidoreduction, using oxygen as hydrogen acceptor is
- Cytochrome oxidase ✔
- Lactate dehydrogenase
- Malate dehydrogenase
- Succinate dehydrogenase
- The enzyme using some other substance, not oxygen as hydrogen acceptor is
- Tyrosinase
- Succinate dehydrogenase
- Uricase✔
- Cytochrome oxidase
- An enzyme which uses hydrogen acceptor as substrate is
- Xanthine oxidase ✔
- Aldehyde oxidase
- Catalase
- Tryptophan oxygenase
- Enzyme involved in joining together two substrates is
- Glutamine synthetase ✔
- Aldolase
- Gunaine deaminase
- Arginase
- The pH optima of most of the enzymes is
- Between 2 and 4
- Between 5 and 9 ✔
- Between 8 and 12
- Above 12
- Coenzymes are
- Heat stable, dialyzable, non protein organic molecules ✔
- Soluble, colloidal, protein molecules
- Structural analogue of enzymes
- Different forms of enzymes
- An example of hydrogen transferring coenzyme is
- CoA
- NAD+ ✔
- Biotin
- TPP
- An examp le of group transferr ing coenzyme is
- NAD+
- NADP+
- FAD
- CoA ✔
- Cocarboxylase is
- Thiamine pyrophosphate ✔
- Pyridoxal phosphate
- Biotin
- CoA
- A coenzyme containing non aromatic hetero ring is
- ATP
- NAD
- FMN
- Biotin ✔
- A coenzyme containing aromatic hetero ring is
- TPP ✔
- Lipoic acid
- Coenzyme Q
- Biotin
- Isoenzymes are
- Chemically, immunologically and electrophoretically different forms of an enzyme ✔
- Different forms of an enzyme similar in all properties
- Catalysing different reactions
- Having the same quaternary structures like the enzyme
- The isoenzymes of LDH
- Differ only in a single amino acid
- Differ in catalytic activity
- Exist in 5 forms depending on M and H monomer contents✔
- Occur as monomers
- Factors affecting enzyme activity:
- Concentration
- pH
- Temperature
- All of these ✔
- ormal serum GOT activity ranges from
- 3.0–15.0 IU/L
- 4.0–17.0 IU/L ✔
- 4.0–60.0 IU/L
- 0.9–4.0 IU/L
- In early stages of myocardial ischemia the most sensitive indicator is the measurement of the activity of
- CPK ✔
- SGPT
- SGOT
- LDH
- Serum acid phosphatase level increases in
- Metastatic carcinoma of prostate ✔
- Myocardial infarction
- Wilson’s disease
- Liver diseases
- Serum a lka l ine phosphatase leve l increases in
- Hypothyroidism
- Carcinoma of prostate
- Hyperparathyroidism ✔
- Myocardial ischemia
- Serum lipase level increases in
- Paget’s disease
- Gaucher’s disease
- Acute pancreatitis ✔
- Diabetes mellitus
- Serum ferroxidase level decreases in
- Gaucher’s disease
- Cirrhosis of liver
- Acute pancreatitis
- Wilson’s disease ✔
- The isoenzymes LDH5 is elevated in
- Myocardial infarction
- Peptic ulcer
- Liver disease ✔
- Infectious diseases
- On the third day of onset of acute myocardial infarction the enzyme elevated is
- Serum AST
- Serum CK
- Serum LDH ✔
- Serum ALT
- LDH1 and LDH2 are elevated in
- Myocardial infarction ✔
- Liver disease
- Kidney disease
- Brain disease
- The CK isoenzymes present in cardiac muscle is
- BB and MB
- MM and MB ✔
- BB only
- MB only
- In acute pancreatitis, the enzyme raised in first five days is
- Serum amylase ✔
- Serum lactic dehydrogenase
- Urinary lipase
- Urinary amylase
- Acute pancreatitis is characterised by
- Lack of synthesis of zymogen enzymes
- Continuous release of zymogen enzymes into the gut
- Premature activation of zymogen enzymes
- Inactivation of zymogen enzymes ✔
- An example of functional plasma enzyme is
- Lipoprotein lipase ✔
- Amylase
- Aminotransferase
- Lactate dehydrogenase
The questions are typically designed to assess the technical skills and knowledge required for the laboratory profession, including the ability to analyze laboratory test results, perform laboratory procedures, and maintain laboratory equipment.
To prepare for these MCQs, candidates should have a thorough understanding of the key concepts and principles of laboratory science. They should also be familiar with common laboratory equipment and procedures, as well as laboratory safety protocols.
Candidates may also benefit from studying specific laboratory science textbooks or taking online courses that cover the material tested in the MCQs. Additionally, practicing sample MCQs and reviewing the answers can help candidates identify areas where they may need to improve their knowledge or skills.
Overall, the MCQs for lab technologists are designed to be challenging and comprehensive, requiring candidates to demonstrate a high level of proficiency in the field of laboratory science.
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