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. 1986 Aug 29;139(1):156-62.
doi: 10.1016/s0006-291x(86)80093-6.

The major excreted protein (MEP) of transformed mouse cells and cathepsin L have similar protease specificity

The major excreted protein (MEP) of transformed mouse cells and cathepsin L have similar protease specificity

S Gal et al. Biochem Biophys Res Commun. .

Abstract

The major excreted protein of transformed mouse cells is an acid activable cysteine protease. In this paper, oxidized insulin B chain is shown to be a substrate for this protease. By isolation and analysis of the insulin B peptides generated by the protease, the bond specificity of this protease was determined. The bonds preferentially cleaved are glu13-ala14, leu17-val18, and tyr26-thr27. No obvious preference for a specific amino acid was found in these studies. The bond specificity of this cysteine protease for oxidized insulin B chain has been compared with that of other proteases, and it is the same as that reported for cathepsin L, suggesting that the major excreted protein and cathepsin L may be the same protein.

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