Purification and separation of multiple forms of lactophorin from bovine milk whey and their immunological and electrophoretic properties.

Purification and separation of multiple forms of lactophorin from bovine milk whey and their immunological and electrophoretic properties.
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从牛乳乳清中纯化和分离多种形式的乳蛋白及其免疫学和电泳特性。

DOI:
10.3168/jds.s0022-0302(89)79181-5
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发表时间:
1989
影响因子:
3.5
通讯作者:
C. Kanno
C. Kanno
中科院分区:
农林科学1区
文献类型:
--
作者:
C. Kanno

文献摘要

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乳蛋白是一种存在于牛乳乳清中的糖蛋白,可与牛乳脂肪球膜可溶性糖蛋白的抗血清发生反应。用DEAE-纤维素(pH7.7)、Sephadex G-100和Bio Gel A-15 m从牛乳乳清蛋白酶-蛋白胨组分的组分3组分中纯化乳蛋白。在pH 8.6的条件下,用DEAE-纤维素柱层析将纯化的乳磷蛋白分离成7个组分。乳磷蛋白的7种组分(LP-1至LP-7)几乎是均一的,但在圆盘电泳上各自的条带有些宽,迁移率不同。在免疫双扩散试验中,这7种乳蛋白组分与乳脂球膜上的抗溶性糖蛋白完全融合,但在免疫电泳中,它们的沉淀线迁移率不同。结果表明,乳磷蛋白有多种形式,但有一组共同的抗可溶性糖蛋白抗原决定簇。
Lactophorin is designated as a glycoprotein, which is present in bovine milk whey and reacts to the antiserum of the soluble glycoprotein of bovine milk fat globule membrane. The lactophorin was purified by DEAE-cellulose (pH 7.7), Sephadex G-100, and then Bio Gel A-15m from the component-3 fraction of the proteose-peptone fraction of bovine milk whey. The purified lactophorin was separated into seven components by DEAE-cellulose chromatography at pH 8.6. The seven components (LP-1 to -7) of lactophorin were almost homogeneous, but the respective bands were somewhat broad and varied in mobilities on disc electrophoresis. The seven lactophorin components fused completely to the antisoluble glycoprotein of milk fat globule membrane on double immunodiffusion but showed different mobilities of precipitation lines on immunoelectrophoresis. The results indicated that lactophorin consisted of multiple forms but had a common set of antigenic determinant groups against anti-soluble glycoprotein.