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一种大豆胰蛋白酶抑制剂。结晶及X射线晶体学研究。

A soybean trypsin inhibitor. Crystallization and x-ray crystallographic study.

作者信息

Hwang D L, Foard D E, Wei C H

出版信息

J Biol Chem. 1977 Feb 10;252(3):1099-101.

PMID:557036
Abstract

Five trypsin and alpha-chymotrypsin inhibitors which have low molecular weights (ranging from 6800 to 8600) and are present in soybean seeds of the Tracy variety have been isolated and purified, and single crystals which give x-ray diffraction data beyond 3-A spacings have been obtained from one of them. The trypsin inhibitor crystallizes in a monoclinic unit cell of symmetry P2(1) and dimensions a = 25.919(7) A, b = 43.23(1) A, c = 19.905(5) A, and beta = 103.63(2) degrees. The assymmetric unit contains 1 molecule of molecular weight 6800. The crystal, which has been found to be unusually stable to x-radiation, has solvent content of approximately 26% by volume.

摘要

已从特雷西品种的大豆种子中分离并纯化出5种分子量较低(范围为6800至8600)的胰蛋白酶和α-胰凝乳蛋白酶抑制剂,并且从其中一种抑制剂中获得了能给出超过3埃间距的X射线衍射数据的单晶。胰蛋白酶抑制剂在对称群为P2(1)的单斜晶胞中结晶,其尺寸为a = 25.919(7)埃,b = 43.23(1)埃,c = 19.905(5)埃,β = 103.63(2)度。不对称单元包含1个分子量为6800的分子。已发现该晶体对X射线异常稳定,其溶剂含量约为26%(体积)。

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