Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
15
|
| pubmed:dateCreated |
1994-5-19
|
| pubmed:abstractText |
The 240-kDa, cGMP-dependent protein kinase substrate protein obtained from porcine aortic smooth muscle, whose phosphorylation was closely associated with stimulation of plasma membrane Ca(2+)-pump ATPase (Yoshida, Y., Sun, H.-T., Cai, J.-Q., and Imai, S. (1991) J. Biol. Chem. 266, 19819-19825), was purified to near homogeneity by three successive chromatographic runs with calmodulin-, concanavalin A-, and heparin-Sepharose columns from microsomes solubilized with Triton X-100. The purified protein was found to bind inositol 1,4,5-trisphosphate (InsP3) in a specific, heparin-inhibitable manner with a Kd of 2.0 nM and Bmax of 450 pmol/mg protein (the binding of inositol 1,3,4,5-tetrakisphosphate was much weaker). In sedimentation experiments on a linear sucrose density gradient the InsP3 binding activity was always with the 240-kDa protein. Protein kinase G phosphorylated the InsP3 receptor purified from the rat cerebellum as well as the 240-kDa protein. Sialic acid content of the protein measured with Limulus polyphemus agglutinin was not significantly different from that of the cerebellar InsP3 receptor. Thus, 240-kDa protein closely resembles InsP3 receptor and may be a type of InsP3 receptor. The only difference was the behavior on SDS-polyacrylamide gel electrophoresis. The 240-kDa protein presented itself as two polypeptides with similar but slightly differing M(r) values, both of which were phosphorylated by protein kinase G.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic GMP-Dependent Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol 1,4,5-Trisphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol 1,4,5-Trisphosphate...,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
269
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
11640-7
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:8157697-Amino Acid Sequence,
pubmed-meshheading:8157697-Animals,
pubmed-meshheading:8157697-Aorta,
pubmed-meshheading:8157697-Calcium Channels,
pubmed-meshheading:8157697-Calmodulin,
pubmed-meshheading:8157697-Centrifugation, Density Gradient,
pubmed-meshheading:8157697-Chromatography, Affinity,
pubmed-meshheading:8157697-Cyclic GMP-Dependent Protein Kinases,
pubmed-meshheading:8157697-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8157697-Inositol 1,4,5-Trisphosphate,
pubmed-meshheading:8157697-Inositol 1,4,5-Trisphosphate Receptors,
pubmed-meshheading:8157697-Kinetics,
pubmed-meshheading:8157697-Microsomes,
pubmed-meshheading:8157697-Molecular Sequence Data,
pubmed-meshheading:8157697-Molecular Weight,
pubmed-meshheading:8157697-Muscle, Smooth, Vascular,
pubmed-meshheading:8157697-Phosphorylation,
pubmed-meshheading:8157697-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:8157697-Substrate Specificity,
pubmed-meshheading:8157697-Swine
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
Purification and characterization of 240-kDa cGMP-dependent protein kinase substrate of vascular smooth muscle. Close resemblance to inositol 1,4,5-trisphosphate receptor.
|
| pubmed:affiliation |
Department of Pharmacology, Niigata University School of Medicine, Japan.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|