Georgopapadakou N H, Smith S A
J Bacteriol. 1985 May;162(2):826-9. doi: 10.1128/jb.162.2.826-829.1985.
The treatment of Candida albicans (yeast form) with digitonin or dimethyl sulfoxide permeabilized cells and caused the activation of chitin synthase in situ. Endogenous activation was completely prevented by the sulfhydryl reagents N-ethylmaleimide, p-chloromercuribenzoate, and 5,5'-dithiobis(2-nitrobenzoic acid); partially prevented by the protease inhibitors antipain, leupeptin, and N alpha-tosyl-L-lysyl chloromethyl ketone; and also partially prevented by EDTA. Thus, a clostripain-like protease may be involved in the endogenous activation phenomenon. The pH activity profile, cofactor requirements, and kinetic parameters of the endogenously activated chitin synthase were identical to those of the trypsin-activated enzyme in protoplast membranes.
用洋地黄皂苷或二甲基亚砜处理白色念珠菌（酵母形式）可使细胞通透，并导致几丁质合酶在原位被激活。巯基试剂N - 乙基马来酰亚胺、对氯汞苯甲酸和5,5'-二硫代双（2 - 硝基苯甲酸）可完全阻止内源性激活；蛋白酶抑制剂抑肽酶、亮抑肽酶和Nα-甲苯磺酰-L-赖氨酰氯甲基酮可部分阻止；EDTA也可部分阻止。因此，一种类梭菌蛋白酶可能参与了内源性激活现象。内源性激活的几丁质合酶的pH活性曲线、辅因子需求和动力学参数与原生质体膜中胰蛋白酶激活的酶相同。
