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山羊β2-微球蛋白的分离与特性

Isolation and properties of goat beta 2-microglobulin.

作者信息

Groves M L, Greenberg R, Farrell H M

出版信息

Comp Biochem Physiol B. 1985;81(3):621-7. doi: 10.1016/0305-0491(85)90376-1.

Abstract

Goat beta 2-microglobulin was isolated and purified from colostrum. Comparisons of the amino acid composition and amino-terminal sequence of the goat protein with the bovine and human homologues, indicates a high degree of similarity. Both goat and bovine beta 2-microglobulins differ slightly in composition from the human molecule, most notably in threonine and proline values. For the first 32 residues, bovine and goat differ only at two positions, one of which is a valyl/isoleucyl substitution consistent with the amino acid compositions. The equivalent goat/human sequence comparison shows seven differences. Immunological studies, using the ELISA method, also confirm the close relatedness of goat and bovine beta 2-microglobulin and their more distant relatedness to the human homologue.

摘要

山羊β2-微球蛋白是从初乳中分离纯化得到的。将山羊蛋白的氨基酸组成和氨基末端序列与牛和人的同源物进行比较,结果显示出高度的相似性。山羊和牛的β2-微球蛋白在组成上与人类分子略有不同,最显著的是苏氨酸和脯氨酸的值。在前32个残基中,牛和山羊仅在两个位置上存在差异,其中之一是缬氨酸/异亮氨酸替代,这与氨基酸组成一致。山羊/人类的等效序列比较显示出七个差异。使用ELISA方法进行的免疫学研究也证实了山羊和牛β2-微球蛋白的密切相关性以及它们与人类同源物的较远相关性。

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