Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 156-162 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 139 |
| Issue number | 1 |
| DOIs | |
| State | Published - Aug 29 1986 |
All Science Journal Classification (ASJC) codes
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
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