rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1988-7-29
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pubmed:abstractText |
We developed a method for immunoaffinity purification of Saccharomyces cerevisiae adenylyl cyclase based on creating a fusion with a small peptide epitope. Using oligonucleotide technology to encode the peptide epitope we constructed a plasmid that expressed the fusion protein from the S. cerevisiae alcohol dehydrogenase promoter ADH1. A monoclonal antibody previously raised against the peptide was used to purify adenylyl cyclase by affinity chromatography. The purified enzyme appeared to be a multisubunit complex consisting of the 200-kilodalton adenylyl cyclase fusion protein and an unidentified 70-kilodalton protein. The purified protein could be activated by RAS proteins. Activation had an absolute requirement for a guanine nucleoside triphosphate.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0270-7306
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2159-65
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2455217-Adenylate Cyclase,
pubmed-meshheading:2455217-Amino Acid Sequence,
pubmed-meshheading:2455217-Antibodies, Monoclonal,
pubmed-meshheading:2455217-Chromatography, Affinity,
pubmed-meshheading:2455217-Epitopes,
pubmed-meshheading:2455217-Fungal Proteins,
pubmed-meshheading:2455217-Guanine Nucleotides,
pubmed-meshheading:2455217-Molecular Sequence Data,
pubmed-meshheading:2455217-Peptides,
pubmed-meshheading:2455217-Recombinant Fusion Proteins,
pubmed-meshheading:2455217-Saccharomyces cerevisiae,
pubmed-meshheading:2455217-ras Proteins
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pubmed:year |
1988
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pubmed:articleTitle |
Purification of a RAS-responsive adenylyl cyclase complex from Saccharomyces cerevisiae by use of an epitope addition method.
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pubmed:affiliation |
Cold Spring Harbor Laboratory, New York 11724.
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pubmed:publicationType |
Journal Article
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