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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
1994-3-1
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pubmed:abstractText |
Chloroflexus aurantiacus J-10-fl was found to contain two types (protease I and protease II) of thermostable proteases which were separated by Butyl-Toyopearl 650 M chromatography. Protease I was purified to electrophoretic homogeneity from the culture broth of C. aurantiacus J-10-fl. The molecular mass of protease I was estimated to be approximately 66 kDa by SDS-PAGE, and the value of approximately 66 kDa was also obtained by the Hedrick-Smith method, indicating that protease I was a monomer. The isoelectric point was 6.2. Protease I activity was inhibited by metalloprotease inhibitors such as EDTA, EGTA, and o-phenanthroline. The optimum pH for the activity of protease I was around 8.0. Addition of Ca2+ increased the pH and heat stabilities of protease I. The activity was stable between pH 4.0-11.0 and up to 75 degrees C, and the maximum activity was observed at 70 degrees C in the presence of 2 mM CaCl2. Protease I was resistant to the treatment by denaturing reagents (8 M urea or 1% SDS) at pH 8.0 and 20 degrees C for 24 h. The sites of cleavage in oxidized insulin B chain by protease I were similar to those by other microbial neutral metalloproteases. Elastase activity of protease I was not detected.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
B
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Chloride,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Pancreatic Elastase,
http://linkedlifedata.com/resource/pubmed/chemical/microbial metalloproteinases
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0916-8451
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
57
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2160-5
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:7764368-Amino Acid Sequence,
pubmed-meshheading:7764368-Bacteria,
pubmed-meshheading:7764368-Calcium Chloride,
pubmed-meshheading:7764368-Chromatography, High Pressure Liquid,
pubmed-meshheading:7764368-Culture Media,
pubmed-meshheading:7764368-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:7764368-Hydrogen-Ion Concentration,
pubmed-meshheading:7764368-Insulin,
pubmed-meshheading:7764368-Isoelectric Point,
pubmed-meshheading:7764368-Metalloendopeptidases,
pubmed-meshheading:7764368-Molecular Sequence Data,
pubmed-meshheading:7764368-Molecular Weight,
pubmed-meshheading:7764368-Pancreatic Elastase,
pubmed-meshheading:7764368-Temperature
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pubmed:year |
1993
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pubmed:articleTitle |
Purification and characterization of a thermostable neutral metalloprotease I from Chloroflexus aurantiacus J-10-fl.
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pubmed:affiliation |
Department of Applied Biological Chemistry, Faculty of Agriculture, Tohoku University, Sendai, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study
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