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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1987-11-5
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pubmed:abstractText |
Renal dipeptidase (dehydropeptidase-I, EC 3.4.13.11) was released from pig kidney membrane preparations by treatment with phosphatidylinositol-specific phospholipase C from Staphylococcus aureus and Bacillus thuringiensis and a phospholipase C preparation from Bacillus cereus to a similar extent as alkaline phosphatase. Endopeptidase-24.11 and aminopeptidase N were not released by this treatment. After treatment of the membrane fraction with the S. aureus phospholipase C the dipeptidase was converted from an amphipathic to a hydrophilic form, as deduced from phase-separation experiments in Triton X-114. It is concluded that renal dipeptidase is anchored to the microvillar membrane by covalently attached phosphatidylinositol.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2822007-14907713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2822007-2422055,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2822007-2432921,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2822007-2865681,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2822007-2865952,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2822007-2959270,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2822007-3011506,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2822007-3028377,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2822007-3548708,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2822007-3780668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2822007-4045459,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2822007-4055788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2822007-588258,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2822007-6119713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2822007-6257680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2822007-6365872,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2822007-6620356,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2822007-7125632,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2822007-7417468
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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 |
Jun
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
244
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
465-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2822007-Animals,
pubmed-meshheading:2822007-Cell Membrane,
pubmed-meshheading:2822007-Cilastatin,
pubmed-meshheading:2822007-Cyclopropanes,
pubmed-meshheading:2822007-Dipeptidases,
pubmed-meshheading:2822007-Kidney,
pubmed-meshheading:2822007-Membrane Proteins,
pubmed-meshheading:2822007-Phosphatidylinositol Diacylglycerol-Lyase,
pubmed-meshheading:2822007-Phosphoinositide Phospholipase C,
pubmed-meshheading:2822007-Phosphoric Diester Hydrolases,
pubmed-meshheading:2822007-Polyethylene Glycols,
pubmed-meshheading:2822007-Swine
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pubmed:year |
1987
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pubmed:articleTitle |
Renal dipeptidase is one of the membrane proteins released by phosphatidylinositol-specific phospholipase C.
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pubmed:affiliation |
Department of Biochemistry, University of Leeds, U.K.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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