| Identification of a novel ATP-dependent proteolytic activity in mitochondrial intermembrane space. | |
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MedLine Citation:
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PMID: 8528150 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The formation of primary amines via proteolysis was monitored in isolated rat liver, kidney cortex and heart mitochondria in the presence and in the absence of ATP. The highest proteolytic activity was detected in kidney cortex mitochondria with about 120 nmoles primary amines/hour x mg protein. The formation rates of liver mitochondria amounted to about 100 nmoles primary amines/hour x mg protein and in heart mitochondria about 60 nmoles primary amines/hour x mg protein. In all mitochondria investigated an ATP-dependent proteolysis of 20-40 nmoles primary amines/hour x mg protein was detected. The effects of various protease inhibitors were tested in rat liver mitochondria and thiol-specific reagents showed a 35-70% inhibition. The ATP stimulable portion of proteolysis was blocked by hemin, a known inhibitor of ATP-dependent proteases. The localization of the proteolytic activity was tested by fractionation of the compartments of rat liver mitochondria using the flourogenic peptide suc-Leu-Leu-Val-Tyr-MCA as substrate. About 90% of the ATP-dependent peptide cleavage activity were found in the mitochondrial intermembrane space. The characteristics of the enzyme were compared to those of other known mitochondrial ATP-dependent proteases and it was concluded that it represents a novel proteolytic system of the intermembrane space. |
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Authors:
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N Sitte; I Drung; W Dubiel |
Publication Detail:
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Type: Comparative Study; Journal Article |
Journal Detail:
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Title: Biochemistry and molecular biology international Volume: 36 ISSN: 1039-9712 ISO Abbreviation: Biochem. Mol. Biol. Int. Publication Date: 1995 Jul |
Date Detail:
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Created Date: 1996-01-29 Completed Date: 1996-01-29 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 9306673 Medline TA: Biochem Mol Biol Int Country: AUSTRALIA |
Other Details:
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Languages: eng Pagination: 871-81 Citation Subset: IM |
Affiliation:
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Institute of Biochemistry, Medical Faculty Charité, Humboldt-University Berlin, Germany. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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ATP-Dependent Proteases Adenosine Triphosphatases / metabolism* Amino Acid Sequence Animals Heat-Shock Proteins / metabolism* Intracellular Membranes / enzymology* Kidney Cortex / enzymology Kinetics Mitochondria / enzymology* Mitochondria, Heart / enzymology Mitochondria, Liver / enzymology, ultrastructure Molecular Sequence Data Rats Rats, Wistar Serine Endopeptidases / metabolism* Subcellular Fractions / enzymology Submitochondrial Particles / enzymology* Substrate Specificity |
| Chemical | |
Reg. No./Substance:
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0/Heat-Shock Proteins; EC 3.4.21.-/ATP-Dependent Proteases; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.-/mitochondrial intermembrane space protease; EC 3.6.1.-/Adenosine Triphosphatases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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