Physicochemical studies on leukocyte alkaline phosphatase.
Leukocyte alkaline phosphatase (ALP) was subjected to polyacrylamide gradient gel electrophoresis and its observed characteristic mobility compared with the ALP of placenta, intestine, liver, and bone. Comparison runs showed that leukocyte ALP moved more anodal to the origin than the others. Physicochemical differences between the leukocyte and other ALP were examined, based on studies of inhibition by L-phenylalanine, L-homoarginine, urea and EDTA, and of heat inactivation. Leukocyte ALP was inhibited strongly by L-homoarginine and urea but not by L-phenylalanine, which seemed similar to the effect of inhibition of liver and bone ALP. However, heat inactivation appeared to be helpful in distinguishing leukocyte from liver and bone ALP.
D000469:Alkaline Phosphatase / Q000097:blood*; D001842:Bone and Bones / Q000201:enzymology; D004492:Edetic Acid / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006709:Homoarginine / Q000494:pharmacology; D006358:Hot Temperature; D006801:Humans; D007422:Intestines / Q000201:enzymology; D007962:Leukocytes / Q000201:enzymology*; D008099:Liver / Q000201:enzymology; D010649:Phenylalanine / Q000494:pharmacology; D010920:Placenta / Q000201:enzymology; D014508:Urea / Q000494:pharmacology
D006709:Homoarginine; D010649:Phenylalanine; D014508:Urea; D004492:Edetic Acid; D000469:Alkaline Phosphatase