Identification of a conserved epitope in class I alcohol dehydrogenase isoenzymes using monoclonal antibodies.
Two monoclonal antibodies raised against native horse alcohol dehydrogenase (HADH) bind preferentially to the enzyme attached to solid supports and recognize the denatured and carboxymethylated HADH subunits. Both antibodies cross-react with the human class I isoenzymes but do not recognize the class III ADH isoenzyme. Protease digestion, electrophoresis and HPLC have been used to identify the linear epitope which is contained in the sequence Pro344-Glu357 of the HADH subunit.
Adinolfi
A
A
International Institute of Genetics and Biophysics, CNR, Naples, Italy.
Leone
N
N
Swallow
D
D
Hopkinson
D A
DA
Zapponi
M C
MC
Ferri
G
G
Camardella
L
L
Ronchi
S
S
D000426:Alcohol Dehydrogenase / Q000737:chemistry / Q000145:classification / Q000276:immunology*; D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D003429:Cross Reactions; D000939:Epitopes / Q000737:chemistry; D006736:Horses; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry / Q000145:classification / Q000276:immunology*; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity
D000911:Antibodies, Monoclonal; D000939:Epitopes; D007527:Isoenzymes; D000426:Alcohol Dehydrogenase