Comparative biochemical study of alkaline phosphatase isozymes in fish, amphibians, reptiles, birds and mammals.
Alkaline phosphatases from the liver, kidney and intestine in various vertebrates were strongly inhibited by beryllium, 2-mercaptoethanol, potassium cyanide and EDTA. The enzymes showed various sensitivities to the inhibition by zinc and to heat denaturation at 56 degrees C for 5 min at pH 7.0. The liver and kidney enzymes showed higher sensitivity to the inhibition by L-homoarginine than by L-phenylalanine. The intestinal enzymes in higher vertebrates were more sensitive to the inhibition by L-phenylalanine than by L-homoarginine, whereas the intestinal ones in lower vertebrates showed quite similar sensitivities to both amino acids.
D000469:Alkaline Phosphatase / Q000378:metabolism*; D000811:Anguilla; D000818:Animals; D002347:Carps; D002645:Chickens; D003370:Coturnix; D007422:Intestines / Q000201:enzymology; D007527:Isoenzymes / Q000378:metabolism*; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008116:Lizards; D051379:Mice; D011892:Rana catesbeiana; D051381:Rats; D012455:Salamandridae; D012911:Snakes; D013045:Species Specificity; D014337:Trout; D014426:Turtles; D014981:Xenopus
D007527:Isoenzymes; D000469:Alkaline Phosphatase