Purification and characterization of a calcium dependent sulfhydryl protease from human platelets
| Autor: | Joseph A. Truglia, Alfred Stracher |
|---|---|
| Rok vydání: | 1981 |
| Předmět: |
Blood Platelets
Protein Conformation medicine.medical_treatment Biophysics chemistry.chemical_element macromolecular substances Calcium Microfilament Biochemistry Substrate Specificity chemistry.chemical_compound Endopeptidases medicine Humans Actin-binding protein Cytoskeleton Molecular Biology Gelsolin Protease biology Molecular mass Leupeptin Microfilament Proteins Cell Biology Actins Molecular Weight EGTA Cysteine Endopeptidases chemistry biology.protein Carrier Proteins |
| Zdroj: | Biochemical and biophysical research communications. 100(2) |
| ISSN: | 0006-291X |
| Popis: | Summary A calcium dependent sulfhydryl protease (CDSP) responsible for over 95% of the neutral protease activity of human platelets has been purified. CDSP is composed of two different polypeptide subunits of molecular weights estimated to be 80,000 and 30,000 daltons. It requires millimolar calcium, reduced sulfhydryl groups and neutral pH for optimal activity. It is inhibited by Leupeptin and an endogenous inhibitor which is removed during purification. CDSP specifically cleaves the platelet's Actin Binding Protein, crosslinker of F-actin microfilaments, into two high molecular weight fragments, the heavier of which still retains its ability to bind to, but not crosslink F-actin into cytoskeletal arrays. |
| Databáze: | OpenAIRE |
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