Molecular cloning and characterization of a cDNA encoding a bovine butanediol dehydrogenase

SMANIA A.M.,; ARGARAÑA C.E.

ELSEVIER SCIENCE BV

Año: 1997 vol. 197 p. 231 - 231

sing a polyclonal antibody against a bovine brain 30-kDa protein (p30), we isolated from a lambda gt11 bovine brain expression library a cDNA that codifies a protein with an apparent molecular mass of 30 kDa. The cDNA nucleotide sequence contained a unique open reading frame encoding a 26.7 kDa polypeptide. The 257 amino acids deduced sequence showed a significant homology with several dehydrogenases, mainly with a bacterial acetoin reductase (62%). The cloned cDNA identity was confirmed by the determination of acetoin reductase activity in lysogens of lambda phage constructions containing the full length cDNA. The results described in this report are to our knowledge the first molecular characterization of a 2,3-butanediol dehydrogenase in mammals.