The heparin–protein complex of ox liver capsule. Isolation and chemical characterization

Author:

Serafini-Fracassini A1,Durward J J1,Floreani L.1

Affiliation:

1. Department of Biochemistry, University of St Andrews, St Andrews, Fife

Abstract

1. A procedure for the isolation and purification of the heparin–protein complex from ox liver capsule, based on the solubility properties of mucopolysaccharide–cetylpyridinium complexes, is described. 2. The yield of the heparin–protein complex with this method averages 35mg./100g. of dry ox liver capsule. 3. The results of analyses on the polysaccharide show good agreement with values previously published for purified heparin fractions. 4. The amino acid analysis of the protein component shows several similarities to that of chondromucoprotein. 5. The results of β-carbonyl elimination, either with or without catalytic hydrogenation, and column chromatography after β-elimination, show that the polysaccharide is covalently bound to the protein.

Publisher

Portland Press Ltd.

Cited by 21 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Heparanase – Discovery and Targets;Advances in Experimental Medicine and Biology;2020

2. Amino acid content of heparins;Journal of Chromatography A;1983-01

3. Isolation and Characterization of Proteoheparan Sulfate from Plasma Membranes of an Ascites Hepatoma, AH 661;The Journal of Biochemistry;1978-08

4. Structure and Biosynthesis of Connective Tissue Proteoglycans;The Glycoconjugates;1978

5. CASCADE EVENTS IN MAST CELL ACTIVATION AND FUNCTION;Molecular Basis of Biological Degradative Processes;1978

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