Ip H S, Orn A, Russell D G, Cross G A
Rockefeller University, New York, NY 10021.
Mol Biochem Parasitol. 1990 May;40(2):163-72. doi: 10.1016/0166-6851(90)90038-n.
Leishmania mexicana, like other species of the genus, has a major 63-kDa surface glycoprotein (gp63) that is an active protease. Reports differ as to whether gp63 is a neutral or an acidic protease. Using three radiolabeled synthetic peptide substrates, gp63 purified from L. m. mexicana is most active at pH 6.5-7.5, in three different buffer systems, and appears to be a sequence-specific endopeptidase. The full extent of sequence specificity is undetermined, but these experiments suggest a strong preference for cleavage at serine or threonine residues. In common with other metalloproteases, the cleavage is on the amino side of the recognition residue.
墨西哥利什曼原虫与该属的其他物种一样，有一种主要的63-kDa表面糖蛋白（gp63），它是一种活性蛋白酶。关于gp63是中性蛋白酶还是酸性蛋白酶，各报告说法不一。使用三种放射性标记的合成肽底物，从墨西哥利什曼原虫中纯化的gp63在三种不同的缓冲系统中，于pH 6.5 - 7.5时活性最高，且似乎是一种序列特异性的内肽酶。序列特异性的完整程度尚未确定，但这些实验表明，它强烈倾向于在丝氨酸或苏氨酸残基处切割。与其他金属蛋白酶一样，切割发生在识别残基的氨基侧。
