| Differential effects of bovine PA28 on six peptidase activities of the lobster muscle proteasome (multicatalytic proteinase). | |
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MedLine Citation:
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PMID: 8554345 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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PA28, an endogenous activator of the bovine proteasome, stimulated the branched-chain amino acid-preferring (BrAAP; 99-fold activation), small-neutral amino acid-preferring (11-fold), acidic chymotrypsin-like (26-fold), and peptidylglutamyl peptide hydrolase (14-fold) activities of the lobster muscle proteasome, while having little or no effect on the trypsin-like, neutral chymotrypsin-like, and caseinolytic activities. These results show that the BrAAP activity, which has been linked to the degradation of myofibrillar proteins by the heat-activated proteasome, is allosterically regulated. However, the activation by PA28 differs from that induced by heat treatment, since heat activation stimulated both the BrAAP and the proteolytic activities but not the other peptidase activities. PA28 shifted the pH optimum of the acidic chymotrypsin-like activity from pH 6-6.5 to pH 7-7.5, while stimulating the activity about 10-fold. These results suggest that PA28 is involved in the activation of the acidic chymotrypsin-like component at physiological pH. |
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Authors:
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D L Mykles |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S. |
Journal Detail:
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Title: Archives of biochemistry and biophysics Volume: 325 ISSN: 0003-9861 ISO Abbreviation: Arch. Biochem. Biophys. Publication Date: 1996 Jan |
Date Detail:
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Created Date: 1996-02-16 Completed Date: 1996-02-16 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 0372430 Medline TA: Arch Biochem Biophys Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 77-81 Citation Subset: IM |
Affiliation:
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Department of Biology, Colorado State University, Fort Collins 80523, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acids
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metabolism Amino Acids, Branched-Chain / metabolism Animals Cattle Chymotrypsin / metabolism Cysteine Endopeptidases / metabolism* Endopeptidases / metabolism* Enzyme Activation Hot Temperature Hydrogen-Ion Concentration Kinetics Multienzyme Complexes / metabolism* Muscles / enzymology* Nephropidae Proteasome Endopeptidase Complex Proteins / pharmacology* Trypsin / metabolism |
| Chemical | |
Reg. No./Substance:
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0/Amino Acids; 0/Amino Acids, Branched-Chain; 0/Multienzyme Complexes; 0/Proteins; EC 3.4.-/Endopeptidases; EC 3.4.21.1/Chymotrypsin; EC 3.4.21.4/Trypsin; 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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