CDNA CLONING AND CHARACTERIZATION OF HUMAN GLYOXALASE-I ISOFORMS FROMHT-1080 CELLS

We have isolated two kinds of cDNA clones encoding glyoxalase I from a human fibrosarcoma HT-1080 cDNA library, One of them is identical to the glyoxalase I cDNA isolated by us, and the other encodes a protein in which alanine at position 111 of the reported sequence for glyoxala se I is replaced by glutamic acid. When the two cDNAs were co-translat ed in vitro, three bands representing two homodimers and one heterodim er appeared on native polyacrylamide gel electrophoresis, as observed for glyoxalase I purified from human erythrocytes or derived from a HT -1080 cell lysate, Escherichia coli cells carrying an expression vecto r of one of the novel glyoxalase I cDNAs showed glyoxalase I activity, These results reveal that two isoforms of human glyoxalase I showing different electrophoretic properties result from a change in one amino acid residue.