Linked Life Data

3162251

Source:http://linkedlifedata.com/resource/pubmed/id/3162251

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1988-4-20
pubmed:abstractText
Careful analysis of affinity-purified class II molecules (Ia Ag) from the murine MHC revealed the existence of a set of associated molecules that consistently co-purified with the Ia Ag. SDS-PAGE revealed that molecules of Mr of 41 to 43 kDa and 56 to 58 kDa were associated with the affinity-purified I-Ak Ag from the AKR B cell lymphoma AKTB-1b. Two-dimensional electrophoresis (IEF vs SDS-PAGE) allowed further characterization of four molecules in the 41- to 43-kDa range and two in the 56- to 58-kDa range. All co-purifying proteins had isoelectric points between 5.2 and 6.2. The specificity of the association of the co-purifying molecules with the I-Ak Ag was established by using two criteria. First, with the exception of actin, proteins co-purifying with the I-Ak molecule were not found in samples of affinity-purified class I (H-2Kk) Ag or membrane Ig from the AKTB-1b lymphoma. Second, the use of the amino group-reactive homobifunctional cross-linker 3,3'-dithiobisproprionimidate with crude membranes from AKTB-1b increased the relative amount of materials co-purifying with I-Ak. The use of the membrane-impermeant cross-linker 3,3'-dithiobis(sulfosuccinimidyl) proprionate provided evidence that the interaction between I-Ak and one or more of the co-purifying components occurs on the cytoplasmic face of the membrane. Two of the co-purifying molecules have been identified. The major material in the 41- to 43-kDa range was partially sequenced, leading to its identification as cytoplasmic actin. One of the components in the 56- to 58-kDa range was tentatively identified as one of the isozymes (RII) of the regulatory subunit of the cAMP-dependent protein kinase, based on the use of the photoaffinity label 8-azido-cAMP.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
140
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1930-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Biochemical characterization of proteins that co-purify with class II antigens of the murine MHC.
pubmed:affiliation
Division of Basic Immunology, National Jewish Center for Immunology and Respiratory Medicine, Denver, CO 80206.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.