دورية أكاديمية
The protein inhibitor of calcium-dependent proteases: purification from bovine heart and possible mechanisms of regulation.
| العنوان: | The protein inhibitor of calcium-dependent proteases: purification from bovine heart and possible mechanisms of regulation. |
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| المؤلفون: | Mellgren RL, Carr TC |
| المصدر: | Archives of biochemistry and biophysics [Arch Biochem Biophys] 1983 Sep; Vol. 225 (2), pp. 779-86. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Country of Publication: United States NLM ID: 0372430 Publication Model: Print Cited Medium: Print ISSN: 0003-9861 (Print) Linking ISSN: 00039861 NLM ISO Abbreviation: Arch Biochem Biophys Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: <2000- > : San Diego, CA : Elsevier Original Publication: New York, NY : Academic Press |
| مواضيع طبية MeSH: | Endopeptidases/*isolation & purification , Glycoproteins/*isolation & purification , Myocardium/*enzymology, Animals ; Calpain ; Cattle ; Cyclic AMP/pharmacology ; Endopeptidases/metabolism ; Glycoproteins/physiology ; Kidney Cortex/enzymology ; Kinetics ; Lysosomes/enzymology ; Muscles/enzymology ; Phosphoprotein Phosphatases/metabolism ; Protein Kinases/metabolism ; Rabbits ; Rats |
| مستخلص: | A bovine heart protein which specifically inhibits calcium-dependent proteases has been purified to near homogeneity. The purified inhibitor had a Stokes radius of 6.8 nm estimated by gel filtration and a molecular weight of 145,000 estimated by sodium dodecyl sulfate-gel electrophoresis. There is evidence that it may be a glycoprotein. The inhibitor could be phosphorylated by bovine heart cyclic AMP-dependent protein kinase, and its inhibitory effect on Peak II (high-calcium-requiring) protease was modestly increased. However, no other phosphorylating or dephosphorylating conditions significantly influenced its activity. The inhibitor was not hydrolyzed by calcium-dependent proteases, but it was very sensitive to proteolytic inactivation by trypsin or proteases present in a lysosomal fraction from rat heart. Thus, proteolysis may represent a mechanism for decreasing the activity of the inhibitor in different physiologic or pathologic conditions. |
| معلومات مُعتمدة: | AM28277 United States AM NIADDK NIH HHS |
| المشرفين على المادة: | 0 (Glycoproteins) 0 (calpain inhibitors) E0399OZS9N (Cyclic AMP) EC 2.7.- (Protein Kinases) EC 3.1.3.16 (Phosphoprotein Phosphatases) EC 3.4.- (Endopeptidases) EC 3.4.22.- (Calpain) |
| تواريخ الأحداث: | Date Created: 19830901 Date Completed: 19831123 Latest Revision: 20190629 |
| رمز التحديث: | 20231215 |
| DOI: | 10.1016/0003-9861(83)90089-9 |
| PMID: | 6312892 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 0003-9861 |
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| DOI: | 10.1016/0003-9861(83)90089-9 |