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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
8
|
| pubmed:dateCreated |
1992-4-14
|
| pubmed:abstractText |
Major and minor isoforms of cyclophilin (CyP-18), a 17.8-kDa protein with peptidyl-prolyl cis-trans isomerase activity, comprise the primary intracellular binding proteins for cyclosporin A. Additional CyP-like proteins with approximate molecular masses of 22 (CyP-22) and 40 kDa (CyP-40) have been recovered from the soluble fraction of calf brain along with CyP-18 by adsorption onto a cyclosporin A affinity column and elution with cyclosporin A. Based on a limited number of peptide sequences from CyP-22, it appears that we have isolated from tissue CyPB, a protein whose sequence was deduced previously from cloned cDNA. The 40-kDa protein was separated from CyP-18 and CyP-22 on a molecular sieving column. Isoelectric focusing of CyP-40 yielded two bands at pI 5.3 and 5.5, in contrast to the basic pI values of CyP-18. Some tryptic peptides from CyP-40 were found to be highly homologous but not identical to bovine CyP-18; others were not significantly homologous to CyP-18 or any other protein in the data base. Unlike the major and minor isoforms of Cyp-18, monospecific polyclonal anti-CyP-18 antibodies did not cross-react with CyP-22 and CyP-40. Likewise, anti-CyP-40 serum minimally cross-reacts with CyP-18 and CyP-22. Cyp-40 possesses peptidyl-prolyl cis-trans isomerase activity which is less sensitive to inhibition by cyclosporin A (IC50 = 300 nM) than is CyP-18 (IC50 = 20 nM).
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclosporins,
http://linkedlifedata.com/resource/pubmed/chemical/Immune Sera,
http://linkedlifedata.com/resource/pubmed/chemical/Peptidylprolyl Isomerase
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
267
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
5503-7
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:1544925-Amino Acid Isomerases,
pubmed-meshheading:1544925-Amino Acid Sequence,
pubmed-meshheading:1544925-Animals,
pubmed-meshheading:1544925-Blotting, Western,
pubmed-meshheading:1544925-Brain,
pubmed-meshheading:1544925-Carrier Proteins,
pubmed-meshheading:1544925-Cattle,
pubmed-meshheading:1544925-Chickens,
pubmed-meshheading:1544925-Chromatography, Affinity,
pubmed-meshheading:1544925-Chromatography, Gel,
pubmed-meshheading:1544925-Cyclosporins,
pubmed-meshheading:1544925-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1544925-Immune Sera,
pubmed-meshheading:1544925-Isoelectric Focusing,
pubmed-meshheading:1544925-Molecular Sequence Data,
pubmed-meshheading:1544925-Molecular Weight,
pubmed-meshheading:1544925-Peptidylprolyl Isomerase,
pubmed-meshheading:1544925-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1544925-Thymus Gland
|
| pubmed:year |
1992
|
| pubmed:articleTitle |
Isolation and characterization of a 40-kDa cyclophilin-related protein.
|
| pubmed:affiliation |
Yale University School of Medicine, New Haven, Connecticut 06510.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|