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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3-4
|
pubmed:dateCreated |
1976-11-21
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pubmed:abstractText |
Double-labeled proteins from rat liver cytosol (14C in long-lived, 3H in short-lived proteins after in-vivo-labeling) are used as substrates for unlabeled proteinases in vitro. Differences in the degradation rates of short-lived and long-lived proteins in vitro by different proteinases and after addition of different effectors allow conclusions concerning their importance for the in-vivo-turnover of substrate proteins. The main activity (greater than 90%) of soluble-lysosomal proteinases at pH 6,1 and pH 6,9 is caused by thiolproteinases, which degrade preferentially short-lived cytosol proteins. These proteinases are inhibited by leupeptin. Autolysis of double-labeled cell fractions shows a remarkably faster breakdown of short-lived substrate proteins only in the soluble part of lysosomes. Microsomal fractions degrade in vitro preferentially long-lived substrate proteins.
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pubmed:language |
ger
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:issn |
0001-5318
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
35
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
301-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:970040-Animals,
pubmed-meshheading:970040-Carbon Radioisotopes,
pubmed-meshheading:970040-Cytosol,
pubmed-meshheading:970040-Isotope Labeling,
pubmed-meshheading:970040-Kinetics,
pubmed-meshheading:970040-Liver,
pubmed-meshheading:970040-Male,
pubmed-meshheading:970040-Peptide Hydrolases,
pubmed-meshheading:970040-Rats,
pubmed-meshheading:970040-Structure-Activity Relationship,
pubmed-meshheading:970040-Subcellular Fractions,
pubmed-meshheading:970040-Tritium
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pubmed:year |
1976
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pubmed:articleTitle |
[Intracellular protein breakdown. VIII. The use of double-labeled proteins as substrates].
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pubmed:publicationType |
Journal Article,
English Abstract
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