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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1976-8-2
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pubmed:abstractText |
1. Phospholipase C [EC 3.1.4.3] found in the growth medium of Streptomyces hachijoensis was purified about sixty-fold by dialysis and column chromatography on Sephadex G-50. 2. The active fraction was separated by isoelectric focusing into two fractions, phospholipase C-I (pI 6.0) and phospholipase C-II (pI 5.6). 3. Both purified phospholipases C were homogeneous by immunodiffusion and were not differentiated as regards antigencity. 4. Phospholipase C-I had maximal activity at pH 8.0 and the optimal temperature was 50degree. Phospholipase C-I was stable at 50degrees for 30 min and was stable at neutral pH. 5. The activity of phospholipase C-I was inhibited by high concentrations of various detergents such as Triton X-100, sodium, cholate, SDS and was also inhibited by Ca2+, Ba2+, Al3+, and EDTA, but was stimulated by Mg2+, and ethyl ether. 6. The Km value of phospholipase C-I was 0.9 mM, using phosphatidylcholine as a substrate. 7. By the gel filtration procedure, the molecular weights of phospholipase C-I and -II were both determined to be 18,000. 8. Phosphatidylcholine, phosphatidylinositol, cardiolipin, sphingomyelin, and lysophosphatidylcholine were hydrolyzed by phospholipase C-I, but phosphatidylethanolamine and phosphatidylserine were hydrolyzed with difficulty under the same conditions, Phospholipase C-I also hydrolyzed phosphatidic acid.
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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/Aluminum,
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Divalent,
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Monovalent,
http://linkedlifedata.com/resource/pubmed/chemical/Detergents,
http://linkedlifedata.com/resource/pubmed/chemical/Edetic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Iron,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-924X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
78
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
537-45
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pubmed:dateRevised |
2007-12-19
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pubmed:meshHeading |
pubmed-meshheading:5411-Aluminum,
pubmed-meshheading:5411-Cations, Divalent,
pubmed-meshheading:5411-Cations, Monovalent,
pubmed-meshheading:5411-Detergents,
pubmed-meshheading:5411-Drug Stability,
pubmed-meshheading:5411-Edetic Acid,
pubmed-meshheading:5411-Hemolysis,
pubmed-meshheading:5411-Hydrogen-Ion Concentration,
pubmed-meshheading:5411-Immunodiffusion,
pubmed-meshheading:5411-Iron,
pubmed-meshheading:5411-Isoenzymes,
pubmed-meshheading:5411-Kinetics,
pubmed-meshheading:5411-Molecular Weight,
pubmed-meshheading:5411-Phospholipases,
pubmed-meshheading:5411-Streptomyces,
pubmed-meshheading:5411-Temperature
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pubmed:year |
1975
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pubmed:articleTitle |
Studies on phospholipases from Streptomyces. III. Purification and properties of Streptomyces hachijoensis phospholipase C.
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pubmed:publicationType |
Journal Article
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