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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
1985-6-10
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pubmed:abstractText |
Protease activity was studied in the frog sciatic nerve. The activity was measured as the release of TCA-soluble radioactivity from either 3H-labelled proteins transported by rapid axonal transport (AXT) or 3H-labelled ganglionic proteins. In nerve homogenates containing transported substrates, protease activity exhibited two peaks, one around pH 5 and one around pH 8. Ca2+ at 100 microM or higher concentrations only stimulated the latter, which was inhibited by 1 mM parachloromercuric benzoate, a sulphydryl reagent, but unaffected by ATP (1 mM). The proteolytic activity was recovered in the 10(5) g supernatant of the homogenate. In desheathed nerves containing 3H-labelled transported proteins, the protease activity could be activated by exposing the nerve to a Ca2+-ionophore, X-537 A, or to an elevated Ca2+-concentration (50 mM). These conditions were also shown to increase the influx and efflux of 45Ca2+ in the nerves. The results indicate the presence within axons of a Ca2+-activated soluble protease, which degrades rapidly transported proteins. The finding that the protease degraded ganglionic soluble proteins to about the same extent suggests a broad substrate specificity. The present system should be useful for further characterization of protease activity during various physiological conditions.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calpain,
http://linkedlifedata.com/resource/pubmed/chemical/Chloromercuribenzoates,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/p-Chloromercuribenzoic Acid
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-8993
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
327
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
29-36
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2985175-Adenosine Triphosphate,
pubmed-meshheading:2985175-Animals,
pubmed-meshheading:2985175-Axons,
pubmed-meshheading:2985175-Biological Transport,
pubmed-meshheading:2985175-Calcium,
pubmed-meshheading:2985175-Calpain,
pubmed-meshheading:2985175-Chloromercuribenzoates,
pubmed-meshheading:2985175-Endopeptidases,
pubmed-meshheading:2985175-Hydrogen-Ion Concentration,
pubmed-meshheading:2985175-Nerve Tissue Proteins,
pubmed-meshheading:2985175-Rana esculenta,
pubmed-meshheading:2985175-Rana temporaria,
pubmed-meshheading:2985175-Sciatic Nerve,
pubmed-meshheading:2985175-Time Factors,
pubmed-meshheading:2985175-Tissue Distribution,
pubmed-meshheading:2985175-p-Chloromercuribenzoic Acid
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pubmed:year |
1985
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pubmed:articleTitle |
Ca2+-activated protease activity in frog sciatic nerve: characterization and effect on rapidly transported axonal proteins.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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