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17 Cards in this Set

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  • Back
What are the two methods to measure glucose in plasma or urine?
Alkaline copper reagent (positive result with any reducing compound)

Glucose oxidase (enzyme) (specific for glucose)
Enzymes are measured by their mass and molarity T/F
FALSE they are measured by their CATALYTIC activity
What are the standard units of enzyme activity?
1 μmol of product formed/min at 30*C
Give three phsysiological ways enzyme activity is regulated in the body
Change in rate of synthesis of the enzyme (slow)

Covalent modification of the enzyme (fast)

Activation by precursors or inhibition by end-products (instantaneous)
Reversible inhibitors bind to the enzyme OR enzyme-substrate complex *covalently* T/F
F, non-covalently
Most reversible inhibitors are highly specific T/F
FALSE, relatively unspecific (will inhibit a number of enzymes)
Most reversible inhibitors are relatively unspecific T/F
T
Reversible inhibitors diffuse onto and off the enzyme, and therefore undergo metabolism and excretion. What is a consequence of this? (Drug wise)
Doses are required relatively frequently
What are the three main types of reversible inhibition?
Competitive
Non-competitive
Uncompetitive
A competitive inhibitor forms an enzyme-inhibitor complex T/F
T (i.e. it competes with the substrate for the formation of the enzyme-substrate complex
A compeitive inhibitor competes with the substrate for the formation of an ESC T/F
T
A competitive inhibitor decreases V(max) T/F
F, V(max) stays the same
A competitive inhibitor increases the apparent K(m) T/F
T
This type of inhibition proceeds to slow formation of the product (i.e. it reduces the rate of reaction at all concentrations of the substrate by interfering with the catalytic mechanism)
Non-competitive inhibition
A non-competitive inhibitor has no effect on the apparent K(m) T/F
T
A non-compeitive inhibitor increases V(max) T/F
F (It decreases)
An uncompetitive inhibitor reduces K(m) and V(max) T/F
T