TY - JOUR
T1 - The major excreted protein (MEP) of transformed mouse cells and cathepsin L have similar protease specificity
AU - Gal, Susannah
AU - Gottesman, Michael M.
N1 - Funding Information:
Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892
PY - 1986/8/29
Y1 - 1986/8/29
N2 - The major excreted protein of transformed mouse cells is an acid activable cysteine protease (1). 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-a1a14, 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.
AB - The major excreted protein of transformed mouse cells is an acid activable cysteine protease (1). 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-a1a14, 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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U2 - 10.1016/S0006-291X(86)80093-6
DO - 10.1016/S0006-291X(86)80093-6
M3 - Article
C2 - 3533059
AN - SCOPUS:0022541361
SN - 0006-291X
VL - 139
SP - 156
EP - 162
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -