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Further characterization of a heat-stable alkaline phosphatase with low sensitivity to L-phenylalanine.

作者信息

Onica D, Rosendahl K, Waldenlind L

机构信息

Department of Clinical Chemistry, Karolinska Institutet, Södersjukhuset Stockholm, Sweden.

出版信息

Clin Chim Acta. 1990 Dec 24;194(2-3):193-202. doi: 10.1016/0009-8981(90)90134-e.

Abstract

A heat-stable alkaline phosphatase, hitherto found in two families with inherited hyperphosphatasemia, was further characterized. The enzyme was similar to serum placental alkaline phosphatase from pregnant women concerning its apparent affinity constant (Km) for 4-nitrophenyl phosphate and its reactivity with H7 monoclonal anti-placental alkaline phosphatase (PLAP) antibodies, but different in the following respects: it exhibited greater heat stability, a higher pH optimum, lower sensitivity to inhibition by L-phenylalanine, and no reactivity with C2 monoclonal anti-PLAP antibodies. The low sensitivity to L-phenylalanine suggests that the enzyme might correspond to a rare phenotype of placental alkaline phosphatase found in human term placenta.

摘要

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