Isolation of pH-optima and apparent Michaelis constants of highly purified enzymes from human and animal sources. Comparison of enzymes of human and animal origin, I.
Enzymes from animal sources are frequently used for quality control of enzyme activity determination in clinical chemistry. For this purpose they should be very similar to human enzymes. It is shown that preparations of enzymes of diagnostic interest from human and porcine organs, purified in exactly the same way, have very similar pH-optima and apparent Michaelis constants for their substrates.
D000410:Alanine Transaminase / Q000378:metabolism; D000818:Animals; D001219:Aspartate Aminotransferases / Q000378:metabolism; D003402:Creatine Kinase / Q000378:metabolism; D004798:Enzymes / Q000302:isolation & purification / Q000378:metabolism*; D005969:Glutamate Dehydrogenase / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D008291:Malate Dehydrogenase / Q000378:metabolism; D009928:Organ Specificity; D013045:Species Specificity; D013552:Swine; D005723:gamma-Glutamyltransferase / Q000378:metabolism
D004798:Enzymes; D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase; D008291:Malate Dehydrogenase; D005969:Glutamate Dehydrogenase; D005723:gamma-Glutamyltransferase; D001219:Aspartate Aminotransferases; D000410:Alanine Transaminase; D003402:Creatine Kinase