Takahashi N, Kurata S, Natori S
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
FEBS Lett. 1993 Nov 15;334(2):153-7. doi: 10.1016/0014-5793(93)81702-2.
A cDNA clone for the 29 kDa proteinase participating in tissue disintegration during metamorphosis of Sarcophaga was isolated. This proteinase, named Sarcophaga cathepsin B, consisted of 256 amino acid residues, and contained three putative N-glycosylation sites. By comparison with other cathepsins B, its unique substrate specificity was partly explained by Ala at position 248.
分离到一个参与肉蝇变态过程中组织分解的29 kDa蛋白酶的cDNA克隆。这种蛋白酶被命名为肉蝇组织蛋白酶B,由256个氨基酸残基组成,并含有三个假定的N-糖基化位点。与其他组织蛋白酶B相比,其独特的底物特异性部分可由248位的丙氨酸来解释。