A cDNA that encodes human H-protein, a constituent protein of the glycine cleavage system, was cloned with anti-rat H-protein antibody as a probe from a human liver cDNA library constructed with an expression vector, λgtll. The longest size of cDNA of the isolated clones was about 750 base long (λHH15B9). On the other hand, we determined the primary structure of human H-protein from the amino terminal Ser by the 12th Val, including a hexapeptide, -Glu-Lys-His-Glu-Trp-Val-. In addition to the finding that most cDNA inserts cloned hybridized with the synthetic DNA probe composed of the possible sequences for the hexapeptide, we confirmed that λHH15B9 encodes the partial primary structure of H-protein in an open reading frame.
|Number of pages||5|
|Journal||Biochemical and biophysical research communications|
|Publication status||Published - 1988 Mar 15|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology