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来自兔骨骼肌的肌动蛋白的一级结构。三种在中性pH下不溶的溴化氰肽。

The primary structure of actin from rabbit skeletal muscle. Three cyanogen bromide peptides that are insoluble at neutral pH.

作者信息

Collins J H, Elzinga M

出版信息

J Biol Chem. 1975 Aug 10;250(15):5906-14.

PMID:238990
Abstract

Three of the 17 peptides produced when actin is treated with cyanogen bromide are sparingly soluble at pH values near neutrality. They were separated from more soluble peptides at pH 6.0 on a column of Sephadex G-10. The soluble peptides were excluded from the gel and emerged at the void volume, while the insoluble peptides were "washed off" by the formic acid in which the sample was applied. The three insoluble peptides were sequenced as a group by studying peptides generated by tryptic and chymotryptic digestion of the mixture, and peptic digestion of the partially resolved peptides. The three peptides are: CB-15 (residues 133 to 176), CB-16 (residues 325 to 354), and CB-17 (residues 191 to 227).

摘要

用溴化氰处理肌动蛋白时产生的17种肽中有3种在接近中性的pH值下微溶。在pH 6.0时,它们在Sephadex G - 10柱上与更易溶的肽分离。可溶性肽被凝胶排除并在空体积处出现,而不溶性肽则被用于溶解样品的甲酸“洗脱”。通过研究该混合物经胰蛋白酶和糜蛋白酶消化产生的肽以及部分分离肽的胃蛋白酶消化产物,将这三种不溶性肽作为一组进行测序。这三种肽分别是:CB - 15(第133至176位氨基酸残基)、CB - 16(第325至354位氨基酸残基)和CB - 17(第191至227位氨基酸残基)。

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