Molecular cloning of a bovine cathepsin
- 1 February 1985
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 225 (3) , 707-712
- https://doi.org/10.1042/bj2250707
Abstract
A cDNA clone for a thiol endoproteinase has been isolated from a bovine heart cDNA library by using a mixture of 32 synthetic oligonucleotides as a hybridization probe. The inserted region is 672 base pairs in length. It contains a sequence encoding the C-terminal region of a protein that is homologous to rat liver cathepsins B and H and to plant thiol proteinases. In addition, it contains the sequence of 442 bases corresponding to the 3′ untranslated region of the mRNA. The inserted region was used as a specific probe in RNA transfer analysis; the size of the mRNA encoding the thiol endoproteinase is estimated to be approx. 1.7 kilobases. Thus, the maximum size of the encoded protein is about 350-400 amino acids.This publication has 40 references indexed in Scilit:
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