| pubmed-article:8755506 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8755506 | lifeskim:mentions | umls-concept:C1171362 | lld:lifeskim |
| pubmed-article:8755506 | lifeskim:mentions | umls-concept:C0031671 | lld:lifeskim |
| pubmed-article:8755506 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:8755506 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:8755506 | lifeskim:mentions | umls-concept:C1515670 | lld:lifeskim |
| pubmed-article:8755506 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:8755506 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:8755506 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:8755506 | lifeskim:mentions | umls-concept:C1305923 | lld:lifeskim |
| pubmed-article:8755506 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:8755506 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
| pubmed-article:8755506 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:8755506 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:8755506 | pubmed:dateCreated | 1996-10-29 | lld:pubmed |
| pubmed-article:8755506 | 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. | lld:pubmed |
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| pubmed-article:8755506 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8755506 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8755506 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8755506 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8755506 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:8755506 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:8755506 | pubmed:author | pubmed-author:CarpenterGG | lld:pubmed |
| pubmed-article:8755506 | pubmed:author | pubmed-author:HorstmanD ADA | lld:pubmed |
| pubmed-article:8755506 | pubmed:author | pubmed-author:DeStefanoKK | lld:pubmed |
| pubmed-article:8755506 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8755506 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:8755506 | pubmed:volume | 93 | lld:pubmed |
| pubmed-article:8755506 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8755506 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8755506 | pubmed:pagination | 7518-21 | lld:pubmed |
| pubmed-article:8755506 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8755506 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8755506 | pubmed:articleTitle | Enhanced phospholipase C-gamma1 activity produced by association of independently expressed X and Y domain polypeptides. | lld:pubmed |
| pubmed-article:8755506 | pubmed:affiliation | Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA. | lld:pubmed |
| pubmed-article:8755506 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8755506 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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