ALKALINE-PHOSPHATASE FROM HUMAN MILK - COMPARISON WITH ISOENZYMES FROM PLACENTA AND LIVER

被引：21

作者：

HAMILTON, TA

GORNICKI, SZ

SUSSMAN, HH

机构：

来源：

BIOCHEMICAL JOURNAL | 1979年 / 177卷 / 01期

关键词：

D O I：

10.1042/bj1770197

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Alkaline phosphatase was partially purified from human milk and its antigenic, functional and structural properties were characterized. By immunochemical and enzymic criteria, the enzyme resembled the alkaline phosphatase isoenzyme found in human liver. Two-dimensional electrophoretic analysis showed that the milk enzyme differed from the liver both in subunit molecular weight and in isoelectric point. These differences were shown to result from variation in sialic acid content.

引用

页码：197 / 201

页数：5

共 22 条

[11]

LOWRY OH, 1951, J BIOL CHEM, V193, P265

[12] AMINO ACID SEQUENCE AROUND REACTIVE SERINE RESIDUE IN ALKALINE PHOSPHATASE FROM ESCHERICHIACOLI [J].