Vitale L, Zubanović M, Abramić M
Acta Biol Med Ger. 1981;40(10-11):1489-95.
The catalytic properties of depeptidyl aminopeptidase and aminopeptidase isolated from human erythrocytes, and the distribution of their activities in different blood cells were determined. Dipeptidyl aminopeptidase was shown to be of the dipeptidyl aminopeptidase III type, activated by Co2+ and inhibited by EDTA, pCMB and partially by DFP and leupeptin. Aminopeptidase preferred Lys-, Phe-, ARg-, and Met-2-naphthylamides as substrates. It was activated by Co2+ and inhibited by EDTA amastatin, bestatin and leupeptin. Dipeptidyl aminopeptidase III activity and aminopeptidase activity on arginine-2-naphthylamide was higher in the population of younger red blood cells. The same activities were also found in thrombocytes, mononuclear and polymorphonuclear leukocytes in concentrations higher than those in erythrocytes.
测定了从人红细胞中分离出的二肽基氨肽酶和氨肽酶的催化特性，以及它们在不同血细胞中的活性分布。结果表明，二肽基氨肽酶属于二肽基氨肽酶III型，受Co2+激活，被EDTA、对氯汞苯甲酸（pCMB）以及部分地被二异丙基氟磷酸（DFP）和亮抑酶肽抑制。氨肽酶优先选择赖氨酸 -、苯丙氨酸 -、精氨酸 - 和甲硫氨酸 - 2 - 萘酰胺作为底物。它受Co2+激活，被EDTA、氨甲酰基亮氨酸（氨肽抑素）、贝司他汀和亮抑酶肽抑制。二肽基氨肽酶III活性以及对精氨酸 - 2 - 萘酰胺的氨肽酶活性在较年轻红细胞群体中更高。在血小板、单核细胞和多形核白细胞中也发现了相同的活性，其浓度高于红细胞中的浓度。
