软骨蛋白聚糖与胶原取代琼脂糖凝胶的相互作用。
Interaction of cartilage proteoglycans with collagen-substituted agarose gels.
作者信息
Greenwald R A, Schwartz C E, Cantor J O
出版信息
Biochem J. 1975 Mar;145(3):601-5. doi: 10.1042/bj1450601.
Abstract
- Rat tail-tendon collagen was coupled to activated Sepharose 4B at 2.5 mg of collagen/ml of gel. Chromatographic columns of this gel were calibrated with T2 virus (Vo) and Dnp-alanine (Vt). 2. The chromatographic behaviour of cartilage proteoglycans on the collagen-substituted gel was studied under conditions of varying ionic strength. Proteoglycan subunit obtained from bovine nasal cartilage, the proteoglycan obtained after digestion with chondroitnase ABC and purified chondriotin sulphate were all retarded on the collagen gel by an interaction that abolished at I0.17. Purified keratan sulphate and hyaluronic acid were not retarded. 3. A strong ionic interaction between cartilage proteoglycan and collagen was demonstrated to depend on the structure of the protein core of the proteoglycan.
摘要
- 将鼠尾腱胶原蛋白以2.5毫克胶原蛋白/毫升凝胶的量偶联到活化的琼脂糖凝胶4B上。用T2病毒（Vo）和二硝基苯丙氨酸（Vt）对该凝胶的色谱柱进行校准。2. 在不同离子强度条件下研究了软骨蛋白聚糖在胶原蛋白替代凝胶上的色谱行为。从牛鼻软骨获得的蛋白聚糖亚基、用软骨素酶ABC消化后得到的蛋白聚糖以及纯化的硫酸软骨素，在胶原蛋白凝胶上均因相互作用而滞留，这种相互作用在离子强度为0.17时消失。纯化的硫酸角质素和透明质酸没有滞留。3. 已证明软骨蛋白聚糖与胶原蛋白之间的强离子相互作用取决于蛋白聚糖蛋白质核心的结构。
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