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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-6
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pubmed:dateCreated |
1988-8-11
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pubmed:abstractText |
Polyclonal antibodies were generated against two synthetic peptides corresponding to sequences from the DNA-binding domain of steroid receptors. The sequence for peptide 1 (13 amino acids) lies between the two putative metal-binding loops of the conserved cysteine region while the sequence for peptide 2 (12 amino acids) lies within one loop. Peptide antibodies were generated by injecting rabbits with peptide conjugated to bovine serum albumin. By Western blot analysis, antibodies to peptide 2 recognized chick and human progesterone receptor and human glucocorticoid receptor, but peptide 1 antibodies did not. No cross-reactivity with native chick progesterone receptor was detected with either anti-peptide. These findings suggest that the epitopes for peptide 2 antibodies, and possibly for peptide 1 antibodies, are inaccessible to antibody in the native receptor.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0022-4731
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-7
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:3386239-Amino Acid Sequence,
pubmed-meshheading:3386239-Animals,
pubmed-meshheading:3386239-Antibodies,
pubmed-meshheading:3386239-Chickens,
pubmed-meshheading:3386239-Cytosol,
pubmed-meshheading:3386239-DNA,
pubmed-meshheading:3386239-Female,
pubmed-meshheading:3386239-HeLa Cells,
pubmed-meshheading:3386239-Humans,
pubmed-meshheading:3386239-Oviducts,
pubmed-meshheading:3386239-Peptide Fragments,
pubmed-meshheading:3386239-Protein Binding,
pubmed-meshheading:3386239-Receptors, Progesterone,
pubmed-meshheading:3386239-Uterus
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pubmed:year |
1988
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pubmed:articleTitle |
Studies with antibodies against the conserved cysteine region of progesterone receptor.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, Mayo Medical School, Rochester, MN 55905.
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pubmed:publicationType |
Journal Article
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