Hiraoka B Y, Fukasawa K, Harada M
Mol Cell Biochem. 1987 Feb;73(2):111-5. doi: 10.1007/BF00219425.
Activation of Streptococcus mitis (ATTC 9811) arginine aminopeptidase resulted in removal of the metal(s) from the enzyme molecule, and the action of the heavy metal ion in the inactivation process was shown to involve formation of a chelate complex between the enzyme molecule and metal or oxidation of functional group(s) on the enzyme surface. The enzyme also underwent activation by bovine serum albumin, amino acids, phosphate, and citric acid, which are probable physiological chelators.
缓症链球菌(ATTC 9811)精氨酸氨基肽酶的激活导致酶分子中的金属被去除,并且重金属离子在失活过程中的作用表明涉及酶分子与金属之间形成螯合物或酶表面官能团的氧化。该酶还可被牛血清白蛋白、氨基酸、磷酸盐和柠檬酸激活,这些物质可能是生理性螯合剂。