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E. Nakazono, Y. Kamata, K. Yamafuji

Determination of the mRNA Sequence of Cathepsin Y, a Cysteine Endopeptidase from Rat Spleen, and Confirmation of Its Ubiquitous

A cysteine endopeptidase from rat spleen was purified, characterized and its gene cloned. This enzyme was originally recognized by its action of producing kininpotentiating peptide from a plasma protein. We named it cathepsin Y due to its localization, acidic pH optimum and the presence of the same set of active site amino acids as in other thiol cathepsins. Here we show the total sequence of the mRNA obtained by means of TaKaRa 5 Full RACE Core Set and complete the previously reported sequence. This completion of the mRNA sequence resulted in the omission of the strangely attached Cterminal peptide from cathepsin Y.

Biological Chemistry, Walter de Gruyter

Print ISSN: 1431-6730
Volume: 383, 12/2002
Pages: 1971 - 1975

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