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土耳其β2-微球蛋白——I. 分离、特性及氨基酸分析。

Turkey beta 2-microglobulin--I. Isolation, properties and amino acid analysis.

作者信息

Lillehoj E, Krutzsch H, Poulik M D

出版信息

Mol Immunol. 1982 Jun;19(6):817-27. doi: 10.1016/0161-5890(82)90008-6.

Abstract

Turkey beta 2-microglobulin (beta 2m) was purified from pooled serum by successive steps of ultrafiltration, gel filtration chromatography, lectin affinity chromatography, anion exchange chromatography, isoelectric focusing and a second step of gel filtration. Identification of turkey beta 2m was based upon NH2-terminal primary structure analysis. The NH2-terminal primary structure of turkey beta 2m is: NH2-Lys-Ile-Glu-Val-Tyr-Ile-Lys-. The purity of the isolated protein was confirmed by two-dimensional polyacrylamide gel electrophoresis, immunodiffusion and immunoelectrophoresis. Physicochemical parameters of turkey beta 2m are: mol. wt, 10,500 (observed), 9959 (calculated); beta electrophoretic mobility; pI, 4.7, 5.2; E1%280, 10.9; absence of terminal D-mannopyranosyl and D-glucopyranosyl residues. Amino acid composition analysis demonstrated similarities between turkey and chicken beta 2ms that distinguished them from mammalian beta 2ms.

摘要

火鸡β2-微球蛋白(β2m)通过超滤、凝胶过滤色谱、凝集素亲和色谱、阴离子交换色谱、等电聚焦以及第二步凝胶过滤等连续步骤从混合血清中纯化得到。火鸡β2m的鉴定基于氨基末端一级结构分析。火鸡β2m的氨基末端一级结构为:NH2-Lys-Ile-Glu-Val-Tyr-Ile-Lys-。通过二维聚丙烯酰胺凝胶电泳、免疫扩散和免疫电泳证实了分离蛋白的纯度。火鸡β2m的物理化学参数为:分子量,10500(实测),9959(计算);β电泳迁移率;pI,4.7,5.2;E1%280,10.9;无末端D-甘露吡喃糖基和D-葡萄糖吡喃糖基残基。氨基酸组成分析表明火鸡和鸡的β2m之间存在相似性,这使它们与哺乳动物的β2m有所区别。

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