Specificity of neuropeptide degradation by two calcium-activated neutral proteases from human skeletal muscle
Autor: | A. M. Kidd, J. R. Mcdermott, David Mantle, J.A. Biggins, K. Davison, B. Lauffart, R. J. T. Pennington |
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Rok vydání: | 1985 |
Předmět: |
Proteases
Size-exclusion chromatography chemistry.chemical_element Neuropeptide Nerve Tissue Proteins Substance P Calcium Dynorphins Chromatography Affinity Sincalide General Biochemistry Genetics and Molecular Biology Gonadotropin-Releasing Hormone chemistry.chemical_compound Endopeptidases medicine Humans Amino Acids General Pharmacology Toxicology and Pharmaceutics Polyacrylamide gel electrophoresis Chromatography High Pressure Liquid Neurotensin chemistry.chemical_classification Calpain Muscles Skeletal muscle General Medicine Chromatography Ion Exchange medicine.anatomical_structure Enzyme Biochemistry chemistry Chromatography Gel Electrophoresis Polyacrylamide Gel |
Zdroj: | Life Sciences. 37:725-730 |
ISSN: | 0024-3205 |
DOI: | 10.1016/0024-3205(85)90542-9 |
Popis: | Two calcium-activated neutral proteases (CAPI & II) were purified from human skeletal muscle by anion exchange, gel filtration and affinity (antipain-Sepharose and Blue Ultrogel A4R) chromatography. The enzymes were homogenous as judged by polyacrylamide gel electrophoresis, and have similar properties with the exception of the Ca2+ concentration required for optimum activity (CAP I = 0.1mM; CAP II = 1mM). Both enzymes hydrolysed a wide variety of neuropeptides. In six cases, the products were separated and identified by hplc and amino acid analysis. Neurotensin was hydrolysed at Tyr3-Glu4; dynorphin1–13 at Arg8Arg9; LHRH at Gly6Leu7; CCK8 at Phe8NH2, substance-P at Met10NH2; somatostatin at Thr10Phe11. Although differences in the rates of neuropeptide degradation were noted for the two CAP's, the specificity was the same for these six peptides. It is suggested that conformational requirements may be more important than side chains adjacent to the cleavage site in directing the specificity of CAP. |
Databáze: | OpenAIRE |
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