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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1981-10-14
|
| pubmed:abstractText |
GM1 ganglioside binding to the crude mitochondrial fraction of rat brain and its effect on (Na+, K+)-ATPase were studied, the following results being obtained: (a) the binding process followed a biphasic kinetics with a break at 50 nM-GM1; GM1 at concentrations below the break was stably associated, while over the break it was loosely associated; (b) stably bound GM1 activated (Na+, K+)-ATPase up to a maximum of 43%; (c) the activation was dependent upon the amount of bound GM1 and was highest at the critical concentration of 20 pmol bound GM1 X mg protein-1; (d) loosely bound GM1 suppressed the activating effect on (Na+, K+)-ATPase elicited by firmly bound GM1; (e) GM1-activated (Na+, K+)-ATPase had the same pH optimum and apparent Km (for ATP) as normal (Na+, K+)-ATPase but a greater apparent Vmax; (f) under identical binding conditions (2 h, 37 degrees C, with 40 nM substance) all tested gangliosides (GM1, GD1a, GD1b, GT1b) activated (Na+, K+)-ATPase (from 26-43%); NeuNAc, sodium dodecylsulphate, sulphatide and cerebroside had only a very slight effect. It is suggested that the ganglioside activation of (Na+-K+)-ATPase is a specific phenomenon not related to the amphiphilic and ionic properties of gangliosides, but due to modifications of the membrane lipid environment surrounding the enzyme.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0022-3042
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
37
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
350-7
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:6267200-Animals,
pubmed-meshheading:6267200-Brain,
pubmed-meshheading:6267200-Enzyme Activation,
pubmed-meshheading:6267200-G(M1) Ganglioside,
pubmed-meshheading:6267200-Gangliosides,
pubmed-meshheading:6267200-Kinetics,
pubmed-meshheading:6267200-Male,
pubmed-meshheading:6267200-Mitochondria,
pubmed-meshheading:6267200-Rats,
pubmed-meshheading:6267200-Sodium-Potassium-Exchanging ATPase,
pubmed-meshheading:6267200-Structure-Activity Relationship
|
| pubmed:year |
1981
|
| pubmed:articleTitle |
Activation of (Na+, K+)-ATPase by nanomolar concentrations of GM1 ganglioside.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|