Interaction of murine monoclonal subunit-specific antibodies with phosphofructokinase-1 from Saccharomyces cerevisiae.
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.
Kopperschläger
G
G
Institute of Biochemistry, Medical Faculty, University of Leipzig, Germany.
Kriegel
T
T
Birkenmeier
G
G
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology / Q000378:metabolism* / Q000494:pharmacology; D000918:Antibody Specificity; D015153:Blotting, Western; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin / Q000378:metabolism; D007700:Kinetics; D046911:Macromolecular Substances; D051379:Mice; D010446:Peptide Fragments / Q000276:immunology; D010732:Phosphofructokinase-1 / Q000276:immunology* / Q000378:metabolism; D011489:Protein Denaturation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D000911:Antibodies, Monoclonal; D046911:Macromolecular Substances; D010446:Peptide Fragments; D010732:Phosphofructokinase-1; D002918:Chymotrypsin