McNab R, Glover L A
Department of Molecular and Cell Biology, University of Aberdeen, U.K.
FEMS Microbiol Lett. 1991 Jul 15;66(1):79-82. doi: 10.1016/0378-1097(91)90424-9.
A cytosolic chitinase (20 kDa by SDS-PAGE) was partially purified from Neurospora crassa. Linear kinetics for enzyme activity were obtained using the substrate [3H]-labelled regenerated chitin, the preparation yielding an apparent Km of 0.965 mg ml-1 and a Vmax of 3.83 micrograms GlcNAc min-1 (mg protein)-1. The enzyme was highly sensitive to allosamidin, an inhibitor of insect chitinase, exhibiting an IC50 of 1.6 microM. Unlike other chitinases that are inhibited by allosamidin, the mode of inhibition of the N. crassa enzyme was shown to be non-competitive.
从粗糙脉孢菌中部分纯化出一种胞质几丁质酶（SDS-PAGE法测定分子量为20 kDa）。使用底物[3H]标记的再生几丁质获得了酶活性的线性动力学，该制剂的表观Km为0.965 mg ml-1，Vmax为3.83微克GlcNAc min-1（mg蛋白）-1。该酶对昆虫几丁质酶抑制剂别洛沙米丁高度敏感，IC50为1.6 microM。与其他被别洛沙米丁抑制的几丁质酶不同，粗糙脉孢菌酶受抑制的模式显示为非竞争性。
