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Molecular cloning and sequencing of cDNA for rat cathepsin H. Homology in pro-peptide regions of cysteine proteinases.

作者信息

Ishidoh K, Imajoh S, Emori Y, Ohno S, Kawasaki H, Minami Y, Kominami E, Katunuma N, Suzuki K

机构信息

Department of Molecular Biology, Tokyo Metropolitan Institute of Medical Science, Japan.

出版信息

FEBS Lett. 1987 Dec 21;226(1):33-7. doi: 10.1016/0014-5793(87)80545-8.

Abstract

A cDNA for rat cathepsin H was isolated and sequenced. The deduced protein comprising 333 amino acid residues is composed of a typical signal sequence (21 residues), a pro-peptide region (92 residues) and a mature enzyme region (220 residues). The amino acid sequence in the pro-peptide region, in particular, residues Phe-(-41) to Ser-(-29) of cathepsin H, is highly homologous to the pro-peptide regions of other cysteine proteinases. This homologous region may play a role in the processing of cysteine proteinases.

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