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软骨素酶的作用。I. 两种不同来源的软骨素酶AC制剂的作用方式。

Action of chondroitinases. I. The mode of action of two chondroitinase-AC preparations of different origin.

作者信息

Hiyama K, Okada S

出版信息

J Biochem. 1976 Dec;80(6):1201-7. doi: 10.1093/oxfordjournals.jbchem.a131390.

DOI:10.1093/oxfordjournals.jbchem.a131390
PMID:138676
Abstract

The modes of action of two chondroitinases-AC [EC 4.2.2.5] from Arthrobacter aurescens and Flavobacterium heparinum were examined. By comparison of the increase of viscosity and by analyses of digests using paper chromatography and gel filtration, it was shown that the Arthrobacter enzyme (A-Chase) degrades the substrate by a stepwise attack, while the Flavobacterium enzyme (F-Chase) exhibits a more random attack, though the first attack of both enzymes is of endo-type. Further study was carried out of the initial rate and final extent of the enzymic degradation of various mucopolysaccharides. The order of the initial rates at which the native mucopolysaccharides are degraded was similar for both enzymes. For A-Chase, the initial rate and final extent of degradation of modified chondroitin sulfate C or chondroitin methyl ester, however, were low compared with those of F-Chase. These results also suggested that A-Chase degrades the substrate by stepwise attack and F-Chase by random attack.

摘要

对来自金色节杆菌和肝素黄杆菌的两种软骨素酶-AC[EC 4.2.2.5]的作用模式进行了研究。通过比较粘度的增加以及使用纸色谱法和凝胶过滤法对消化产物进行分析,结果表明,节杆菌酶(A-Chase)通过逐步攻击降解底物,而黄杆菌酶(F-Chase)表现出更随机的攻击,尽管两种酶的首次攻击都是内切型的。对各种粘多糖的酶促降解的初始速率和最终程度进行了进一步研究。两种酶对天然粘多糖的降解初始速率顺序相似。然而,对于A-Chase,修饰的硫酸软骨素C或软骨素甲酯的降解初始速率和最终程度与F-Chase相比很低。这些结果还表明,A-Chase通过逐步攻击降解底物,F-Chase通过随机攻击降解底物。

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Action of chondroitinases. I. The mode of action of two chondroitinase-AC preparations of different origin.软骨素酶的作用。I. 两种不同来源的软骨素酶AC制剂的作用方式。
J Biochem. 1976 Dec;80(6):1201-7. doi: 10.1093/oxfordjournals.jbchem.a131390.
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Isolation of a neural chondroitin sulfate proteoglycan with neurite outgrowth promoting properties.
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J Cell Biol. 1994 Aug;126(3):783-99. doi: 10.1083/jcb.126.3.783.
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