| Interaction of human erythrocyte multicatalytic proteinase with polycations. | |
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MedLine Citation:
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PMID: 2378899 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The multicatalytic proteinase from human erythrocytes (macropain, proteasome) is a large enzyme composed of at least six distinct subunits ranging in molecular masses from 20 to 30 kDa. As its name implies, this proteinase appears to contain multiple catalytic sites with differing specificities toward peptide substrates. Several polycationic substances, including polylysines, polyarginine, protamine and histone H1 markedly stimulated caseinolytic activity of the proteinase. Activation was instantaneous, and involved increasing the Vmax of the proteinase for casein. Prolonged preincubation with polylysine at 37 degrees C resulted in autolytic inactivation of the proteinase. The polylysine concentrations required for half-maximal activation or autolytic inactivation were the same. A 23 kDa subunit of the proteinase disappeared at the same rate as loss of catalytic activity, and with the same pH dependence and polylysine concentration dependence. These results suggest that polylysine perturbs the structure of the multicatalytic proteinase, resulting in increased catalytic activity toward substrates; and, with prolonged exposure, allowing autoproteolytic inactivation to occur. The 23 kDa subunit appeared to be required for expression of caseinolytic activity, and may therefore be a catalytic subunit of the complex having activity against casein. |
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Authors:
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R L Mellgren |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 1040 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 1990 Aug |
Date Detail:
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Created Date: 1990-09-07 Completed Date: 1990-09-07 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 28-34 Citation Subset: IM |
Affiliation:
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Department of Pharmacology and Therapeutics, Medical College of Ohio, Toledo 43699-0008. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Chromatography, Gel Chromatography, Ion Exchange Cysteine Endopeptidases / blood*, isolation & purification Enzyme Activation Erythrocytes / enzymology* Histones / pharmacology Humans Kinetics Molecular Weight Multienzyme Complexes / blood*, isolation & purification Peptides / pharmacology Polylysine / pharmacology Protamines / pharmacology Protease Inhibitors / pharmacology Proteasome Endopeptidase Complex Spermine / pharmacology |
| Grant Support | |
ID/Acronym/Agency:
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HL 36573/HL/NHLBI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Histones; 0/Multienzyme Complexes; 0/Peptides; 0/Protamines; 0/Protease Inhibitors; 25104-18-1/Polylysine; 25212-18-4/polyarginine; 71-44-3/Spermine; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.25.1/Proteasome Endopeptidase Complex |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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