Linked Life Data

8253806

Source:http://linkedlifedata.com/resource/pubmed/id/8253806

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
35
pubmed:dateCreated
1994-1-13
pubmed:abstractText
L-29, a mammalian soluble lactose-binding lectin, was previously shown to be phosphorylated in confluent 3T3 fibroblasts (Cowles, E. A., Agrwal, N., Anderson, R. L., and Wang, J. L. (1990) J. Biol. Chem. 265, 17706-17712), which contain a small amount of this protein. We have determined the site of phosphorylation on L-29, taking advantage of the abundance of L-29 (about 1% of total soluble cell protein) in confluent polarized Madin-Darby canine kidney (MDCK) cells. Approximately 15-20% of the L-29 is phosphorylated in these cells. Phosphoamino acid analysis showed phosphate incorporation only at serine. Analysis of chymotryptic and endoproteinase Asp-N-generated NH2-terminal fragments by Edman degradation showed that 90% of the phosphate was at Ser6 and 10% at Ser12. The sequence surrounding Ser6, which is conserved in all known L-29 sequences, indicated that this serine might be phosphorylated by casein kinase I or casein kinase II. Reaction of human recombinant L-29 with [gamma-32P]ATP and each of these casein kinases showed that only casein kinase I catalyzed significant incorporation of 32P into L-29; and, as with the L-29 from the MDCK cell extracts, most of the phosphate was incorporated at Ser6 and a small amount was incorporated at Ser12.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
26712-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
L-29, a soluble lactose-binding lectin, is phosphorylated on serine 6 and serine 12 in vivo and by casein kinase I.
pubmed:affiliation
Department of Psychiatry, University of California, San Francisco 94143.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't