伴刀豆球蛋白A的发光特性。

The luminescence properties of concanavalin A.

Miller J N, Nwokedi G I

Biochim Biophys Acta. 1975 Jun 26;393(2):426-34. doi: 10.1016/0005-2795(75)90071-9.

Abstract

The luminescence properties of native concanavalin A, both at room temperature and at 77 degrees K, are similar to those of other proteins containing tyrosine and tryptophan. 2. Binding of methyl alpha-D-glucopyranoside to concanavalin A causes a slight reduction of its fluorescence at room temperature. 3. Removal of Mn2+ and Ca2+ ions from concanavalin A causes a small increase in its fluoresence. The fluorescence: phosphorescence ratio and phosphorescence lifetime of apo-concanavalin A are similar to those of tryptophan. 4. Denaturation of concanavalin A by urea and by guanidine hydrochloride apparently takes place in two stages. Apo-concanavalin A is more easily denatured than the native molecule, but concavalin A combined with methyl alpha-D-glucopyranoside is more resistant to denaturation. 5. The luminescence properties of concanavalin A are pH-dependent. 6. The results have been interpreted in terms of the known structure and properties of concanavalin A.

摘要

天然伴刀豆球蛋白A在室温及77K时的发光特性与其他含酪氨酸和色氨酸的蛋白质相似。2. α-D-甲基吡喃葡萄糖苷与伴刀豆球蛋白A结合会使其在室温下的荧光略有减弱。3. 从伴刀豆球蛋白A中去除Mn2+和Ca2+离子会使其荧光略有增加。脱辅基伴刀豆球蛋白A的荧光：磷光比率及磷光寿命与色氨酸的相似。4. 尿素和盐酸胍对伴刀豆球蛋白A的变性作用显然分两个阶段进行。脱辅基伴刀豆球蛋白A比天然分子更容易变性，但与α-D-甲基吡喃葡萄糖苷结合的伴刀豆球蛋白A对变性更具抗性。5. 伴刀豆球蛋白A的发光特性依赖于pH值。6. 已根据伴刀豆球蛋白A的已知结构和特性对这些结果进行了解释。