Proteolytic fragmentation of myosin: location of SH-1 and SH-2 thiols
| Autor: | R. Cardinaud |
|---|---|
| Rok vydání: | 1979 |
| Předmět: |
Macromolecular Substances
Protein Conformation Peptide Myosins Biochemistry Divalent Protein structure Myosin medicine Animals Chymotrypsin Trypsin Sulfhydryl Compounds Polyacrylamide gel electrophoresis Edetic Acid chemistry.chemical_classification biology Proteolytic enzymes Sodium Dodecyl Sulfate General Medicine Peptide Fragments chemistry biology.protein Calcium Electrophoresis Polyacrylamide Gel Rabbits medicine.drug |
| Zdroj: | Biochimie. 61:807-821 |
| ISSN: | 0300-9084 |
| DOI: | 10.1016/s0300-9084(79)80275-8 |
| Popis: | The heavy chain fragmentation pattern of native myosin when digested by proteolytic enzymes is influenced by such conditions as the nature of the proteolytic agent, ionic strength and presence or absence of divalent cations. HMM and S-1 produced by digestion of 14CNEM-labelled myosin under various conditions were analyzed by sodium dodecyl-sulfate polyacrylamide gel electrophoresis. Purified samples of these species were digested under controlled conditions by chymotrypsin and trypsin and a comparison of the observed heavy chain fragmentation patterns led to a sequential arrangement of the proteolytic fragments. The main features of this arrangement are the following: a 21K molecular weight tryptic peptide is found at the N-terminal side of myosin heavy chain. Adjacent to it is a 48K peptide, then a 19.5K peptide containing the two SH-1 and SH-2 thiols. These three peptides constitute the heavy chain of S-1. Adjacent to this S-1 heavy chain is a tryptic (and also chymotryptic) 40K peptide. The rest of the HMM heavy chain on the C-terminus is a sequence susceptible to both chymotrypsin and trypsin attack yielding an undefined number of small peptides. |
| Databáze: | OpenAIRE |
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