rdf:type |
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lifeskim:mentions |
|
pubmed:issue |
1-2
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pubmed:dateCreated |
1995-5-30
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pubmed:abstractText |
Murine monoclonal subunit-specific antibodies against heterooctameric phosphofructokinase-1 from Saccharomyces cerevisiae exhibiting no cross-reactivity were purified and characterized regarding complex formation with the native enzyme, immunological reactivity to the SDS-denatured subunits originating from native and proteolytically truncated phosphofructokinase, and protection against proteolytic degradation. Strong complex formation was found with one alpha-specific antibody. Western blotting employing different enzyme forms allowed to localize epitope sites of the alpha-polypeptide chain. Monoclonal antibodies protect phosphofructokinase-1 against chymotryptic degradation.
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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:month |
Apr
|
pubmed:issn |
0014-5793
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
17
|
pubmed:volume |
363
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
17-21
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:7729541-Animals,
pubmed-meshheading:7729541-Antibodies, Monoclonal,
pubmed-meshheading:7729541-Antibody Specificity,
pubmed-meshheading:7729541-Blotting, Western,
pubmed-meshheading:7729541-Chromatography, Gel,
pubmed-meshheading:7729541-Chromatography, High Pressure Liquid,
pubmed-meshheading:7729541-Chymotrypsin,
pubmed-meshheading:7729541-Kinetics,
pubmed-meshheading:7729541-Macromolecular Substances,
pubmed-meshheading:7729541-Mice,
pubmed-meshheading:7729541-Peptide Fragments,
pubmed-meshheading:7729541-Phosphofructokinase-1,
pubmed-meshheading:7729541-Protein Denaturation,
pubmed-meshheading:7729541-Saccharomyces cerevisiae
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pubmed:year |
1995
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pubmed:articleTitle |
Interaction of murine monoclonal subunit-specific antibodies with phosphofructokinase-1 from Saccharomyces cerevisiae.
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pubmed:affiliation |
Institute of Biochemistry, Medical Faculty, University of Leipzig, Germany.
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pubmed:publicationType |
Journal Article
|