Yonezawa S, Takahashi T, Ichinose M, Miki K, Tanaka J, Gasa S
Department of Zoology, Faculty of Science, Hokkaido University, Sapporo, Japan.
Biochem Biophys Res Commun. 1990 Jan 30;166(2):1032-8. doi: 10.1016/0006-291x(90)90914-9.
The amino-terminal structure of rat gastric cathepsin E was identified and compared with the corresponding regions of human procathepsin E and other aspartic proteinases. The alignment revealed that cathepsin E has the most extended amino-terminal structure in aspartic proteinases, thus suggesting that the activation peptide (propeptide) of the human enzyme is 39-residues long. Analysis of oligosaccharide units suggested that rat cathepsin E possesses one N-linked carbohydrate unit, probably of the high mannose type. No evidence was obtained for the presence of O-linked sugars in rat cathepsin E.
确定了大鼠胃组织组织蛋白酶E的氨基末端结构，并将其与人类组织蛋白酶E原及其他天冬氨酸蛋白酶的相应区域进行比较。序列比对显示，组织蛋白酶E在天冬氨酸蛋白酶中具有最长的氨基末端结构，由此表明人类该酶的激活肽（前肽）长度为39个氨基酸残基。对寡糖单元的分析表明，大鼠组织蛋白酶E含有一个N-连接的碳水化合物单元，可能是高甘露糖型。未获得大鼠组织蛋白酶E存在O-连接糖的证据。
