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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1994-10-13
|
| pubmed:abstractText |
Glycosylphosphatidylinositol(GPI) anchor-hydrolyzing phospholipases include C- and D-type phospholipases and have been described in a number of organisms including bacteria, protozoan parasites, plants, and mammals. Although these phospholipases efficiently cleave GPI structures in vitro, the physiological role of GPI hydrolysis by anchor-specific phospholipases is still unclear. In order to permit comparison of the known GPI anchor-hydrolyzing phospholipases, we studied the kinetic parameters of these enzymes and provide an overview of the currently available information.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0100-879X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
27
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
369-74
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading | |
| pubmed:year |
1994
|
| pubmed:articleTitle |
GPI anchor-hydrolyzing phospholipases.
|
| pubmed:affiliation |
Institute of Biochemistry and Molecular Biology, University of Bern, Switzerland.
|
| pubmed:publicationType |
Journal Article
|