Nakamura T, Shibata Y, Fujimura S
Department of Oral Microbiology, Matsumoto Dental College, Nagano-Prefecture, Japan.
J Clin Microbiol. 1988 May;26(5):1070-1. doi: 10.1128/jcm.26.5.1070-1071.1988.
Heparinase (heparin lyase, EC 4.2.2.7) was isolated from the cell extract of an oral bacterium, Bacteroides heparinolyticus. It was a basic protein with an isoelectric point of 9.5. Its molecular weight was 63,000. The enzyme was the most active against heparin among the tested mucopolysaccharides. Catalytic properties may be similar to those of heparinase of Flavobacterium heparinum, since the enzymatic degradation products obtained by using the two enzymes were the same on the basis of paper chromatography.
肝素酶（肝素裂解酶，EC 4.2.2.7）是从口腔细菌解肝素拟杆菌的细胞提取物中分离得到的。它是一种碱性蛋白质，等电点为9.5。其分子量为63,000。在测试的粘多糖中，该酶对肝素的活性最高。由于基于纸色谱法，使用这两种酶获得的酶促降解产物相同，因此其催化特性可能与解肝素黄杆菌的肝素酶相似。
