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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1983-7-8
|
| pubmed:abstractText |
Octameric malate synthase is located in the glyoxysomes of cucumber cotyledons. The enzyme is predominantly confined to the organelle's membrane and can be solubilized with Mg2+. Separation of cell structures in a zonal rotor afforded, besides glyoxysomes, two other zones with malate synthase activity, viz., in the gradient supernatant and in the range of the endoplasmic reticulum (ER). Malate synthases of these three fractions were purified to apparent homogeneity and classified according to their molecular weight. Differences in subunit molecular weight, however, could not be detected when malate synthases from the three fractions were compared. Mature malate synthase, as well as malate synthase prepared from fractions sedimenting similarly to the ER, exhibited the following behavior with respect to aggregation and deaggregation: at low salt concentrations and in the absence of Mg2+, the enzyme shifted to aggregated forms (approx 100 S); with 2 mM Mg2+, malate synthase deaggregated and occurred predominantly as an octamer (19 S). By changing buffer conditions, mature forms of malate synthase could be interconverted repeatedly between octameric and aggregated forms, whereas a monomeric form (5 S), prepared from soluble fractions assigned to the cytosol, did not oligomerize. The amphipathic properties of malate synthase were demonstrated by the enzyme's capacity for binding phospholipids.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0003-9861
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
223
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
618-28
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading | |
| pubmed:year |
1983
|
| pubmed:articleTitle |
Malate synthase: aggregation, deaggregation, and binding of phospholipids.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|