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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
35
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pubmed:dateCreated |
1992-1-17
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pubmed:abstractText |
We have isolated from chicken embryos a novel 53-kDa protein possessing properties which are similar, but not identical to the 55-kDa PDI polypeptide from chicken embryos. The novel 53-kDa polypeptide copurifies with PDI, but is separated by ion-exchange chromatography. The novel 53-kDa polypeptide cross-reacts strongly with antibodies specific for bovine PDI and cross-reacts to varying degrees with six different preparations of antibodies specific for chicken PDI which is identical to the beta-subunit of chicken prolyl 4-hydroxylase. Anti-bovine PDI immunoglobulins selected by the purified 53-kDa polypeptide react with bovine PDI but not with the beta-subunit of prolyl 4-hydroxylase, suggesting that the 53-kDa polypeptide shares epitopes with bovine PDI but not with the chicken prolyl 4-hydroxylase beta-subunit. Amino acid compositional analysis of the purified polypeptide yielded unique data when compared to PDI and other PDI-like polypeptides. Edman degradation from the N terminus of the 53-kDa polypeptide yields a sequence very different from the N terminus of PDI. This sequence is unique when compared to all entries in available databases. A 20-residue sequence of an internal cyanogen bromide fragment of the 53-kDa polypeptide gives a nearly identical match with human beta-endorphin. The 53-kDa polypeptide is capable of cleaving the disulphides of insulin under conditions where PDI is active. The periodic acid-Schiff assay failed to detect bound carbohydrate. These observations support evidence for a family of PDI-like proteins in chicken embryo and suggest that PDI activity is not confined to only one protein.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulins,
http://linkedlifedata.com/resource/pubmed/chemical/Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Procollagen-Proline Dioxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Disulfide-Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Endorphin
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
|
pubmed:volume |
266
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
23732-8
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:1660884-Amino Acid Sequence,
pubmed-meshheading:1660884-Animals,
pubmed-meshheading:1660884-Chick Embryo,
pubmed-meshheading:1660884-Cross Reactions,
pubmed-meshheading:1660884-Humans,
pubmed-meshheading:1660884-Immunoglobulins,
pubmed-meshheading:1660884-Isomerases,
pubmed-meshheading:1660884-Macromolecular Substances,
pubmed-meshheading:1660884-Molecular Sequence Data,
pubmed-meshheading:1660884-Molecular Weight,
pubmed-meshheading:1660884-Peptide Fragments,
pubmed-meshheading:1660884-Peptides,
pubmed-meshheading:1660884-Procollagen-Proline Dioxygenase,
pubmed-meshheading:1660884-Protein Disulfide-Isomerases,
pubmed-meshheading:1660884-Rabbits,
pubmed-meshheading:1660884-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1660884-beta-Endorphin
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pubmed:year |
1991
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pubmed:articleTitle |
A novel 53-kDa polypeptide from chicken embryo.
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pubmed:affiliation |
Department of Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway 08854.
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pubmed:publicationType |
Journal Article,
Comparative Study
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