TY - JOUR
T1 - Cloning of cDNA encoding human H-protein, a constituent of the glycine cleavage system
AU - Hiraga, Koichi
AU - Kure, Shigeo
AU - Yamamoto, Masayuki
AU - Ishiguro, Yoshihisa
AU - Suzuki, Tamio
PY - 1988/3/15
Y1 - 1988/3/15
N2 - 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.
AB - 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.
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U2 - 10.1016/S0006-291X(88)80345-0
DO - 10.1016/S0006-291X(88)80345-0
M3 - Article
C2 - 3348809
AN - SCOPUS:0023818715
SN - 0006-291X
VL - 151
SP - 758
EP - 762
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -