对软体动物脉红螺血蓝蛋白结构单元1的一项具有挑战性的见解。

A challenging insight on the structural unit 1 of molluscan Rapana venosa hemocyanin.

作者信息

Dolashka-Angelova Pavlina, Stevanovic Stefan, Dolashki Alexandar, Devreese Bart, Tzvetkova Bonka, Voelter Wolfgang, Van Beeumen Jozef, Salvato Benedetto

机构信息

Institute of Organic Chemistry, Bulgarian Academy of Sciences, G. Bonchev 9, Sofia 1113, Bulgaria.

出版信息

Arch Biochem Biophys. 2007 Mar 1;459(1):50-8. doi: 10.1016/j.abb.2006.12.009. Epub 2007 Jan 22.

DOI:10.1016/j.abb.2006.12.009

PMID:17291443

Abstract

Hemocyanins of mollusks are high molecular mass glycoproteins with a complex quaternary structure which still remains to be defined in detail for most of its species as far as number, spatial distribution and interactions of their structural units is concerned. In the present study, we isolated the functional units of the structural subunit RvH1 of Rapana venosa hemocyanin, combining enzymatic and non-enzymatic methods. Our results suggest that Hc's carbohydrate moieties play a basic role in the organization of the structural units, resulting from post-translational polymerization of the 50 kDa functional units and involving sugar moieties that link between them.

摘要

软体动物的血蓝蛋白是具有复杂四级结构的高分子量糖蛋白，就其结构单元的数量、空间分布和相互作用而言，大多数物种的四级结构仍有待详细确定。在本研究中，我们结合酶促和非酶促方法，分离出了脉红螺血蓝蛋白结构亚基RvH1的功能单元。我们的结果表明，血蓝蛋白的碳水化合物部分在结构单元的组织中起基本作用，这是由50 kDa功能单元的翻译后聚合产生的，并且涉及连接它们的糖部分。