Hamilton T A, Górnicki S Z, Sussman H H
Biochem J. 1979 Jan 1;177(1):197-201. doi: 10.1042/bj1770197.
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.
从人乳中部分纯化了碱性磷酸酶，并对其抗原性、功能和结构特性进行了表征。根据免疫化学和酶学标准，该酶类似于在人肝脏中发现的碱性磷酸酶同工酶。二维电泳分析表明，乳中的酶在亚基分子量和等电点方面均与肝脏中的酶不同。这些差异被证明是由唾液酸含量的变化引起的。
