化学
动力学
酶
降级(电信)
色谱法
酶动力学
生物化学
立体化学
活动站点
计算机科学
量子力学
电信
物理
作者
Frode Haugen,Fritz Kortner,Bjørn Larsen
标识
DOI:10.1016/0008-6215(90)84280-8
摘要
Purified preparations of alginate lyase from Klebsiella aerogenes and Haliotis sp. were investigated for activity and degradation patterns with alginate and alginate fragments having different compositions and sequences. With fragments approaching homopolymers of guluronate and mannuronate, Michaelis-Menten kinetics were obeyed and kinetic parameters could be obtained. Degradation of alginates containing all four possible linkages in various proportions, followed by isolation of the fragments and identification of the end groups by n.m.r. spectroscopy, indicated that the enzyme preparations can attack more than one type of linkage. The results are discussed with reference to the concept of specificity for enzymes with copolymeric substrates having non-regular distributions of units.
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