ACTION PATTERN OF POLYSACCHARIDE LYASES ON GLYCOSAMINOGLYCANS
ACTION PATTERN OF POLYSACCHARIDE LYASES ON GLYCOSAMINOGLYCANS
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DOI：
10.1093/glycob/4.3.289
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发表时间：
1994-06-01
期刊：
影响因子：
4.3
通讯作者：
LINHARDT, RJ
中科院分区：
文献类型：
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作者：
JANDIK, KA;GU, KA;LINHARDT, RJ
使用粘度测量和梯度聚丙烯酰胺凝胶电泳 (PAGE) 检查多糖裂解酶对糖胺聚糖底物的作用模式。肝素裂解酶 I（肝素酶，EC 4.2.2.7）和肝素裂解酶 II（无 EC 编号）均以随机内溶方式作用于肝素。肝素裂解酶 II 对硫酸乙酰肝素表现出理想的内溶作用模式，而肝素裂解酶 I 降低硫酸乙酰肝素分子量的速度较慢。肝素裂解酶Ri（肝素酶，EC 4.2.2.8）仅对硫酸乙酰肝素起内溶作用，并且不裂解肝素。来自普通变形杆菌的软骨素 ABC 裂解酶（软骨素酶 ABC，EC 4.2.2.4）以几乎相同的初始速率内溶作用于 6-硫酸软骨素（硫酸软骨素 C）和硫酸皮肤素，但以降低的速率作用于 4-硫酸软骨素（硫酸软骨素 A），从而进一步降低其分子量慢慢地。针对软骨素-4-和-6-硫酸盐检查了两种软骨素AC裂解酶（软骨素酶AC，均为EC 4.2.2.5）。来自金黄色节杆菌的软骨素 AC 裂解酶 A 对 4- 和 -6-硫酸软骨素的胞解作用通过粘度测定法得到证明，并使用梯度 PAGE 和凝胶渗透色谱法进行了证实。来自肝素黄杆菌 (Cytophagia heparinia) 的软骨素 AC 裂解酶 F 对相同的底物产生内溶作用。来自肝素肝素的软骨素 B 裂解酶（软骨素酶 B，无 EC 编号）对硫酸皮肤素进行内溶作用，给出与作用于硫酸皮肤素的软骨素 ABC 裂解酶几乎相同的作用模式。
The action pattern of polysaccharide lyases on glycosaminoglycan substrates was examined using viscosimetric measurements and gradient polyacrylamide gel electrophoresis (PAGE). Heparin lyase I (heparinase, EC 4.2.2.7) and heparin lyase II (no EC number) both acted on heparin in a random endolytic fashion. Heparin lyase II showed an ideal endolytic action pattern on heparan sulphate, while heparin lyase I decreased the molecular weight of heparan sulphate more slowly. Heparin lyase Ri (heparitinase, EC 4.2.2.8) acted endolytically only on heparan sulphate and did not cleave heparin. Chondroitin ABC lyase (chondroitinase ABC, EC 4.2.2.4) from Proteus vulgaris acted endolytically on chondroitin-6-sulphate (chondroitin sulphate C) and dermatan sulphate at nearly identical initial rates, but acted on chondroitin-4-sulphate (chondroitin sulphate A) at a reduced rate, decreasing its molecular weight much more slowly. Two chondroitin AC lyases (chondroitinase AC, both EC 4.2.2.5) were examined towards chondroitin-4- and -6-sulphates. The exolytic action of chondroitin AC lyase A from Arthrobacter aurescens on both chondroitin-4- and -6-sulphates was demonstrated viscosimetrically and confirmed using both gradient PAGE and gel permeation chromatography. Chondroitin AC lyase F from Flavobacterium heparinum (Cytophagia heparinia) acted endolytically on the same substrates. Chondroitin B lyase (chondroitinase B, no EC number) from F.heparinum acted endolytically on dermatan sulphate giving a nearly identical action pattern as observed for chondroitin ABC lyase acting on dermatan sulphate.