Linked Life Data

3435528

Source:http://linkedlifedata.com/resource/pubmed/id/3435528

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-3-8
pubmed:abstractText
A protein in calf serum with molecular mass of 125,000 is selectively phosphorylated by the surface kinase activity of intact tissue culture cells and erythrocytes. The protein, termed pp125, is phosphorylated at serine and threonine residues to a ratio of greater than 1 mol P/mol. The pp125 is an acidic protein (pI 4.4) which also serves as substrate for purified phosvitin/casein kinases but not for cyclic AMP-dependent protein kinases. About 80-fold purification of pp125 was achieved by ion exchange and affinity chromatography. Gel filtration under non-reducing conditions showed that pp125 is part of a complex (Mr 535,000). The pp125 obviously originates from a large plasma protein: the incubation of calf plasma with intact cells in the presence of [gamma-32P]ATP resulted in the labeling of a protein with Mr greater than 300,000 (pp greater than 300). The relationship between pp greater than 300 in plasma and pp125 in serum was demonstrated by cyanogen bromide peptide patterns, and the use of specific anti-serum raised against pp125. Furthermore, it was shown that pp125 is derived from pp greater than 300 during blood clotting.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0158-5231
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
349-57
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Substrates for the cell surface protein kinase in blood: a calf serum protein and its precursor in plasma.
pubmed:affiliation
Institute of Experimental Pathology, German Cancer Research Center, Heidelberg, Federal Republic of Germany.
pubmed:publicationType
Journal Article