Ilg T, Harbecke D, Overath P
Max-Planck-Institut für Biologie, Tübingen, Germany.
FEBS Lett. 1993 Jul 19;327(1):103-7. doi: 10.1016/0014-5793(93)81049-6.
Leishmania mexicana amastigotes express a lysosomal protein, which is antigenically related to the promastigote surface metalloproteinase (gp63). It is shown that the purified gp63-related protein from amastigote is also an active metalloproteinase. The pH-optimum of the enzyme is acidic, similar to lysosomal cysteine proteinases, but distinct from the neutral to basic pH-optimum of the promastigote surface proteinase. This study appears to be the first report on a metalloproteinase with a lysosomal localization.
墨西哥利什曼原虫无鞭毛体表达一种溶酶体蛋白,该蛋白与前鞭毛体表面金属蛋白酶(gp63)存在抗原相关性。研究表明,从无鞭毛体中纯化出的与gp63相关的蛋白也是一种活性金属蛋白酶。该酶的最适pH为酸性,类似于溶酶体半胱氨酸蛋白酶,但不同于前鞭毛体表面蛋白酶的中性至碱性最适pH。本研究似乎是关于一种定位于溶酶体的金属蛋白酶的首次报道。