Linked Life Data

6281275

Source:http://linkedlifedata.com/resource/pubmed/id/6281275

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1982-7-22
pubmed:abstractText
The phosphorylation of a 55,000-dalton protein (Protein IIIb) present in mammalian brain was previously shown to be increased by depolarizing agents in the presence of calcium, by cyclic nucleotides, and by appropriate neurotransmitters. We now report that Protein IIIb has been purified 660-fold to near homogeneity and partially characterized. The hydrodynamic properties of the purified protein indicate that it exists as an elongated monomer. cAMP-dependent protein kinase catalyzes the incorporation of 0.82 mol of phosphate into serine/mol of protein. The protein is heterogeneous in isoelectric focusing, exhibiting multiple forms with isoelectric points ranging in pH from 6.6 to 7.3.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
257
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6524-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Purification and characterization of protein IIIb, a mammalian brain phosphoprotein.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't