INTERACTION BETWEEN ENDOGENOUS CIRCULATING SULFATED-GLYCOSAMINOGLYCANS AND PLASMA-PROTEINS

被引：12

作者：

PASQUALI, F ^{[1
]}

OLDANI, C ^{[1
]}

RUGGIERO, M ^{[1
]}

MAGNELLI, L ^{[1
]}

CHIARUGI, V ^{[1
]}

VANNUCCHI, S ^{[1
]}

机构：

[1] IST PATOL GEN FIRENZE,VIALE MORGAGNI 50,I-50134 FLORENCE,ITALY

来源：

CLINICA CHIMICA ACTA | 1990年 / 192卷 / 01期

关键词：

Glycosamicoglycan; Plasma; Plasma protein;

D O I：

10.1016/0009-8981(90)90267-V

中图分类号：

R446 [实验室诊断]; R-33 [实验医学、医学实验];

学科分类号：

1001 ;

摘要：

Interaction between endogenous 35S-labelled plasma glycosaminoglycans and proteins in murine plasma was demonstrated by coelution from gel chromatography of circulating 35S-labelled glycosaminoglycans with a wide range of plasma proteins. Autoradiography of electrophoretic tracing of proteins from 35S-sulfate labelled plasma showed that labelled glycosaminoglycans were associated with alpha1, alpha2, beta globulins and albumin, but not with gamma globulins. Analysis by gel chromatography on Sepharose CL-6B of delipidated 35S-labelled plasma after either proteolysis or beta-elimination, suggested that 35S-labelled glycosaminoglycan chains were covalently bound to proteins. Lipids were probably involved in the supramolecular assembly of GAGs with plasma proteins, as shown by hydrophobic interaction chromatography. In addition, strong, non-covalent interaction between glycosaminoglycan chains and proteins was responsible for the difficulty in extracting 'free' glycosaminoglycans from plasma. Consistently, ion-exchange chromatography of 35S-sulfate labelled delipidated plasma after alkali treatment, revealed that the anionic properties of glycosaminoglycans were hampered when plasma proteins were present. © 1990.

引用

页码：19 / 27

页数：9

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