Peptide bond cleavage site determination of novel proteolytic enzymes found in ROS 17/2.8 cell lysates
| Autor: | Dana Perrin, Patricia Harrison, Peter T. Guidon |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Physiology
Molecular Sequence Data Clinical Biochemistry Biology Cleavage (embryo) Substrate Specificity Cleave Tumor Cells Cultured Animals Peptide bond Amino Acid Sequence Phosphorylation Protein kinase A Polyacrylamide gel electrophoresis Protein Kinase C Osteoblasts Proteolytic enzymes Cell Biology Peptide Fragments Culture Media Rats Biochemistry Cell culture Oligopeptides Peptide Hydrolases |
| Zdroj: | Journal of Cellular Physiology. 166:407-412 |
| ISSN: | 1097-4652 0021-9541 |
| DOI: | 10.1002/(sici)1097-4652(199602)166:2<407::aid-jcp19>3.0.co;2-7 |
| Popis: | We have identified proteolytic activities in the rat osteoblastic osteosarcoma cell line ROS 17/2.8 which are capable of cleaving a peptide substrate for protein kinase C-mediated phosphorylation (PSPKC, Pro-Leu-Ser-Arg-Thr-Leu-Ser-Val-Ala-Ala-Lys). Using polyacrylamide gel electrophoresis conditions similar to those used to resolve small molecular weight proteins, the peptide bonds of PSPKC which are cleaved by the proteolytic activities present in ROS 17/2.8 cell lysates have been determined. These activities cleave the Ser-Arg, Thr-Leu, and Ser-Val peptide bonds. To date, no proteolytic activities present in osteoblast cell lysates have been described with the aforementioned peptide bond specificities, suggesting that these activities are novel. The PSPKC-cleaved peptide fragment pattern generated was similar for several different osteoblast cell lysates. Lysates generated from different rat tissues were also able to cleave PSPKC, but the peptide fragment pattern generated by ROS 17/2.8 cell lysates appeared to be unique amongst these tissues. © 1996 Wiley-Liss, Inc. |
| Databáze: | OpenAIRE |
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