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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1985-7-9
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pubmed:abstractText |
A thiol protease has been isolated and purified from the postribosomal fraction of encysted embryos of the brine shrimp Artemia using a six-step procedure. The purified enzyme has a molecular weight of 55,000 +/- 4,200 and is composed of subunits of Mr 31,500 +/- 559 and 25,867 +/- 1,087. Isoelectric focusing revealed two discrete bands, one at pH 4.6 and the other at pH 5.1. The protease appears to be a member of the thiol group of proteases based on its inhibition by leupeptin, antipain, chymostatin, Ep-475, and several other thiol protease inhibitors. The enzyme was stimulated by heavy metal chelators and thiol reagents. At pH 3.5-4.0 the thiol protease hydrolyzed a wide range of proteins including bovine serum albumin, hemoglobin, Artemia embryo soluble proteins, Artemia lipovitelline, and protamine, whereas at pH 6.0-6.5 the enzyme showed a high degree of specificity for Artemia elongation factor 2 and lipovitelline alpha 1. The total amount of protease activity in crude homogenates of Artemia embryos decreased by about 50% during the first 24 h of development, while the amount of free, active enzyme decreased proportionally for 9 h of development then remained constant during the next 26-27 h of development. These changes in protease activity appear to reflect changing levels of an endogenous protease inhibitor during development.
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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/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Egg Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Egg Proteins, Dietary,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Hemoglobins,
http://linkedlifedata.com/resource/pubmed/chemical/Protamines,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin, Bovine,
http://linkedlifedata.com/resource/pubmed/chemical/lipovitellin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
260
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7008-14
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3888992-Animals,
pubmed-meshheading:3888992-Artemia,
pubmed-meshheading:3888992-Cysteine Endopeptidases,
pubmed-meshheading:3888992-Cytosol,
pubmed-meshheading:3888992-Egg Proteins,
pubmed-meshheading:3888992-Egg Proteins, Dietary,
pubmed-meshheading:3888992-Endopeptidases,
pubmed-meshheading:3888992-Hemoglobins,
pubmed-meshheading:3888992-Isoelectric Point,
pubmed-meshheading:3888992-Molecular Weight,
pubmed-meshheading:3888992-Protamines,
pubmed-meshheading:3888992-Serum Albumin, Bovine
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pubmed:year |
1985
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pubmed:articleTitle |
Purification and characterization of a cytosol protease from dormant cysts of the brine shrimp Artemia.
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pubmed:publicationType |
Journal Article
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