[Identification of serum alkaline phosphatase from human bone].
Polyacrylamide gel electrophoresis utilizing sodium dodecyl sulfate followed by specific staining for alkaline phosphatase was accomplished using sera from patients with osteosarcoma, polyostotic fibrous dysplasia, metastatic bone tumor, and idiopathic hyper-alkalinephosphatasemia. Alkaline phosphatase activity of the sera was uniformly demonstrated at a molecular weight of 60,000. L-homoarginine more strongly inhibited the alkaline phosphatase activity than did L-phenylalanine. Alkaline phosphatase activity was markedly inactivated by heating. Regarding substrate specificity, the hydrolysis of p-nitro-phenylphosphate occurred at a lower rate than did that of phenylphosphate. By contrast, the hydrolysis of alpha- and beta-glycerophosphate occurred at a higher rate than did that of phenylphosphate. As seen from the data presented here, the serum alkaline phosphatase samples obtained from these patients with skeletal disorders have several common characteristics.
Shinozaki
T
T
Department of Orthopaedic Surgery, Gunma University School of Medicine, Japan.
Chigira
M
M
Udagawa
E
E
D000469:Alkaline Phosphatase / Q000037:antagonists & inhibitors / Q000097:blood* / Q000378:metabolism; D001842:Bone and Bones / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D006709:Homoarginine / Q000494:pharmacology; D006801:Humans; D008970:Molecular Weight; D010649:Phenylalanine / Q000494:pharmacology; D013379:Substrate Specificity
D006709:Homoarginine; D010649:Phenylalanine; D000469:Alkaline Phosphatase