Enzymes Flashcards
Catalyst
A substance that enhances chemical reactions but is not altered by the reaction
Substances that are structurally similar to the substrate and will compete with the substrate for the enzye
Competitive inhibitor’s
Proteins that act as catalyst to accelerate chemical reactions within cells
Enzyme
A substance that An enzyme acts upon
Substrate
Substances that will interfere with the activity of the enzyme
Inhibitors
Enzymes that can perform catalytic activity without assistance from another substrate
Simple enzymes
Enzyme poisons or in activator such as heavy metals or halogen
Non-competitive inhibitor’s
Enzymes that require the presence Of a non-protein component to function
Conjugated enzymes
Non-protein components that conjugate with enzymes to carry out its function usually a metal
Cofactor
True or false all enzymes are found inside sales
True
True or false all enzymes are proteins and are affected by the same things that affect any other proteins
True
True or false each enzyme has multiple substrate it up acts upon
False Bitch
Transfer of electrons from one molecule to another
Oxidoreductases
Transfer is functional groups from one molecule to another
Transferases
Hydrolyzes a chemical bond
Hydrolases & lysases
Catalyzes the structural formation of isomers
Isomerases
Join together sugar phosphate backbone of DNA fragments
Ligases
List of five variables that can affect enzymatic reaction
Timing temperature PH inhibitors and concentration of reaction
An increase of _____ C what affect the enzyme reaction rate
10 degrees
True or false enzymes are measured in usual concentration units
False
Increase in______ Enzyme levels indicate cellular death and leakage of the enzyme from the sale
LDH
What LBH fraction is increased in myocardial infarction and in some hemolytic anemia
LDH 1 & LDH2
What do enzymes are considered to be the major cardiac enzymes
LDH &CK
What enzyme is a cellular enzyme with a physiological role associated with the adenosine triphosphate generation for contractile or transport systems and is responsible for the production creatine phosphate?
Creatine Kinase
What CKI so enzyme is present in heart muscles and in the diaphragm and esophagus
CKMB
What enzyme functions to break down complex carbohydrate molecules such as starches by splitting the chemical bonds in the molecular chain
Analyses
Functions to remove the ternal phosphate group from inorganic phosphate Ester and an alkaline solution is found in lower concentrations in liver and placental tissue
ALP
Belongs to a group of eight times known as Aminotransferase and found I am practically every tissue in the body it is in particularly high concentration in liver and cardiac tissues intermediate in skeletal muscle and the kidney and low in most other tissues
AST
Catalyzes the transfer of an amino group between L alamine and L glutamate High concentrations occur in the liver in relatively low concentrations are found in the heart muscle and kidney
ALT
Glutathione is the common substrate of this enzyme in the body present in high concentrations and liver kidney pancreas and prostate
GGT
Assay in which once the substrate and enzyme are mixed they are allowed to react for a set period of time the reaction is stopped and one absorbance reading is taken
Fixed time assay
Mid portion of reaction we are the most accurate measurements are taken
Linear phase
Final stage of enzymatic reaction where the enzyme have utilize all of the substrate unsuitable for taking measurements
Substrate depletion\exhaustion
Assays begin with a known amount of substrate and measure the amount of substrate that remains after a given period of time
Substrate used up assay
Assay in which the progress or rate of the reaction is measured over a period of time multiple absorbance readings are taken at preset timed intervals
Kinetic assay
Assays are designed to allow enzymes in the patient specimen to react with a set amount of substrate and quantitate the amount of product formed
Product formed assay
The initial period of a reaction where the substrate buffer and cofactors factors are mixed kinetic equilibrium is established
Lag phase
Monosaccharides or dissect liberated by amylases reaction with the substrate are measured. Byproducts of amylase action are reducing the substances the enzyme action is directly proportional to the amount of reducing substance produced
Saccharogenic method
A dye is coupled to a complex and soluble polysaccharide. The sample is incubated and after a fixed time the color liberated from the dye is split from the original complex and the amount measured the enzyme accent is directly proportional to the amount of color produced
Chromolytic Method
A different approach to a chromolytic technique depends on the release of a small water soluble fragment in such a way that the color can be measured continuously reaction is monitored by measurement of liberated chromogen
Continuous monitoring
Amos is allowed to act on it starch substrate to which iodine has been attached. Hydrolysis of the starch molecule occurs and iodine is released resulting in a decrease of the initial dark blue color intensity. The greater the Amaylase effectivity the lighter the color of the final solution
Amyloclastic method
