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从人初乳中分离β2-微球蛋白(作者译)

[Isolation of beta2-microglobulin from human colostrum (author's transl)].

作者信息

Haupt H, Baudner S

出版信息

Hoppe Seylers Z Physiol Chem. 1975 May;356(5):577-81.

PMID:50996
Abstract

The beta2-microglobulin from human colostrum was purified by a combination of ordinary protein-chemical techniques: gel filtration, ion-exchange chromatography and zone electrophoresis. The procedure is organized in such a way that the simultaneous isolation of many other milk proteins is possible. The beta2-microglobulin obtained from colostrum cannot be distinguished by physical-chemical or immunological means from the beta2-microblobulin isolated from the urine of patients with kidney-tubule diseases. At the beginning of lactation, human milk contains significantly more than 10 mg/-100 ml beta2-microglobulin, but the concentration drops within two or three days to 15-30% of the original amount.

摘要

人初乳中的β2-微球蛋白通过常规蛋白质化学技术相结合的方法进行纯化:凝胶过滤、离子交换色谱法和区带电泳。该程序的组织方式使得同时分离许多其他乳蛋白成为可能。从初乳中获得的β2-微球蛋白,用物理化学或免疫学方法无法与从肾小管疾病患者尿液中分离出的β2-微球蛋白区分开来。在哺乳初期,人乳中β2-微球蛋白的含量明显超过10毫克/100毫升,但在两到三天内浓度降至原来的15%-30%。

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