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体内组织蛋白酶原L向组织蛋白酶L的多重加工过程。

Multiple processing of procathepsin L to cathepsin L in vivo.

作者信息

Ishidoh K, Saido T C, Kawashima S, Hirose M, Watanabe S, Sato N, Kominami E

机构信息

Department of Biochemistry, Juntendo University School of Medicine, 2-1-1 Hongo, Bunkyo-ku, Tokyo, 113, Japan.

出版信息

Biochem Biophys Res Commun. 1998 Nov 9;252(1):202-7. doi: 10.1006/bbrc.1998.9613.

Abstract

Three amino-terminal-specific peptidic antibodies against cathepsin L were generated. These antibodies recognize in vitro processing products of procathepsin L in time-course-dependent fashion. Immunoblot analyses with these antibodies followed by immunoprecipitation with anti-cathepsin L antibody showed that the amino terminal amino acid sequences of intracellular cathepsin L are heterogeneous: the single chain form of cathepsin L starts with either EPLML, LKIPK or IPKSV, and the heavy chain of the two chain form with IPKSV. Percoll density gradient and fluorescence immunohistochemistry suggested that these three species of cathepsin L localize in the lysosomes where procathepsin L processing occurs.

摘要

制备了三种针对组织蛋白酶L的氨基末端特异性肽抗体。这些抗体以时间依赖性方式识别组织蛋白酶L原的体外加工产物。用这些抗体进行免疫印迹分析,随后用抗组织蛋白酶L抗体进行免疫沉淀,结果表明细胞内组织蛋白酶L的氨基末端氨基酸序列是异质的:组织蛋白酶L的单链形式起始于EPLML、LKIPK或IPKSV,而双链形式的重链起始于IPKSV。Percoll密度梯度和荧光免疫组织化学表明,这三种组织蛋白酶L定位于发生组织蛋白酶L原加工的溶酶体中。

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