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rdf:type |
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lifeskim:mentions |
umls-concept:C0004083,
umls-concept:C0017262,
umls-concept:C0031671,
umls-concept:C0441655,
umls-concept:C1171362,
umls-concept:C1305923,
umls-concept:C1514562,
umls-concept:C1515670,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2349975
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pubmed:issue |
15
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pubmed:dateCreated |
1996-10-29
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pubmed:abstractText |
The X and Y domains of phospholipase C (PLC)-gamma1, which are conserved in all mammalian phosphoinositide-specific PLC isoforms and are proposed to interact to form the catalytic site, have been expressed as individual hexahistidine-tagged fusion proteins in the baculovirus system. Following coinfection of insect cells with recombinant viruses, association of X and Y polypeptides was demonstrated in coprecipitation assays. When enzyme activity was examined, neither domain possessed catalytic activity when expressed alone; however, coexpression of the X and Y polypeptides produced a functional enzyme. This reconstituted phospholipase activity remained completely dependent on the presence of free Ca2+. The specific activity of the X:Y complex was significantly greater (20- to 100-fold) than that of holoPLC-gamma1 and was only moderately influenced by varying the concentration of substrate. The enzyme activities of holoPLC-gamma1 and the X:Y complex exhibited distinct pH optima. For holoPLC-gamma1 maximal activity was detected at pH 5.0, while activity of the X:Y complex was maximal at pH 7.2.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-1310981,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-1316902,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-1328245,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-1396585,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-1659758,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-1683701,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-1700866,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-1708916,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-2557343,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-3022313,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-3040753,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-3254788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-7504950,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-7528537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-7531435,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-7642515,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-7663162,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-7717996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-8013457,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-8093003,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-8132610,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-8206897,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-8386625,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-8408058,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8755506-8430079
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
93
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7518-21
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8755506-Amino Acid Sequence,
pubmed-meshheading:8755506-Animals,
pubmed-meshheading:8755506-Binding Sites,
pubmed-meshheading:8755506-Cell Line,
pubmed-meshheading:8755506-Conserved Sequence,
pubmed-meshheading:8755506-Histidine,
pubmed-meshheading:8755506-Isoenzymes,
pubmed-meshheading:8755506-Kinetics,
pubmed-meshheading:8755506-Macromolecular Substances,
pubmed-meshheading:8755506-Mammals,
pubmed-meshheading:8755506-Phosphatidylinositol 4,5-Diphosphate,
pubmed-meshheading:8755506-Phospholipase C gamma,
pubmed-meshheading:8755506-Rats,
pubmed-meshheading:8755506-Recombinant Fusion Proteins,
pubmed-meshheading:8755506-Sequence Tagged Sites,
pubmed-meshheading:8755506-Spodoptera,
pubmed-meshheading:8755506-Transfection,
pubmed-meshheading:8755506-Type C Phospholipases
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pubmed:year |
1996
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pubmed:articleTitle |
Enhanced phospholipase C-gamma1 activity produced by association of independently expressed X and Y domain polypeptides.
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pubmed:affiliation |
Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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