相思子凝集素色氨酸残基的研究。修饰的停流动力学及荧光猝灭研究。

Studies on tryptophan residues of Abrus agglutinin. Stopped-flow kinetics of modification and fluorescence-quenching studies.

作者信息

Patanjali S R, Swamy M J, Surolia A

出版信息

Biochem J. 1987 Apr 1;243(1):79-86. doi: 10.1042/bj2430079.

DOI:10.1042/bj2430079

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1147817/

Abstract

The presence of two essential tryptophan residues/molecule was implicated in the binding site of Abrus agglutinin [Patanjali, Swamy, Anantharam, Khan & Surolia (1984) Biochem. J. 217, 773-781]. A detailed study of the stopped-flow kinetics of the oxidation of tryptophan residues revealed three classes of tryptophan residues in the native protein. A discrete reorganization of tryptophan residues revealed three classes of tryptophan residues in the native protein. A discrete reorganization of tryptophan residues into two phases was observed upon ligand binding. The heterogeneity of tryptophan exposure was substantiated by quenching studies with acrylamide, succinimide and Cs+. Our study revealed the microenvironment of tryptophan residues to be hydrophobic, and also the presence of acidic amino acid residues in the vicinity of surface-localized tryptophan residues.

摘要

两个必需的色氨酸残基/分子的存在与相思豆凝集素的结合位点有关[帕坦加利、斯瓦米、阿南塔拉姆、汗和苏罗利亚（1984年）《生物化学杂志》217卷，773 - 781页]。对色氨酸残基氧化的停流动力学的详细研究揭示了天然蛋白质中有三类色氨酸残基。色氨酸残基的离散重组揭示了天然蛋白质中有三类色氨酸残基。配体结合后观察到色氨酸残基分为两个阶段的离散重组。用丙烯酰胺、琥珀酰亚胺和Cs +进行的猝灭研究证实了色氨酸暴露的异质性。我们的研究表明色氨酸残基的微环境是疏水的，并且在表面定位的色氨酸残基附近也存在酸性氨基酸残基。

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