title: Cloning of cDNA encoding human H-protein, a constituent of the glycine cleavage system.
abstract: 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, lambda gt11. The longest size of cDNA of the isolated clones was about 750 base long (lambda HH15B9). 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 lambda HH15B9 encodes the partial primary structure of H-protein in an open reading frame.
authors.affiliation: Department of Biochemistry, Toyama Medical and Pharmaceutical, University School of Medicine, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Hiraga
authors.forename: S
authors.initials: S
authors.lastname: Kure
authors.forename: M
authors.initials: M
authors.lastname: Yamamoto
authors.forename: Y
authors.initials: Y
authors.lastname: Ishiguro
authors.forename: T
authors.initials: T
authors.lastname: Suzuki
mesh_terms: D000594:Amino Acid Oxidoreductases; D000595:Amino Acid Sequence; D001483:Base Sequence; D002352:Carrier Proteins / Q000235:genetics* / Q000302:isolation & purification; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D005998:Glycine / Q000378:metabolism; D050961:Glycine Decarboxylase Complex H-Protein; D050841:Glycine Dehydrogenase (Decarboxylating); D006801:Humans; D008099:Liver / Q000378:metabolism*; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000235:genetics
chemical_list: D002352:Carrier Proteins; D050961:Glycine Decarboxylase Complex H-Protein; D012333:RNA, Messenger; D004247:DNA; D000594:Amino Acid Oxidoreductases; D050841:Glycine Dehydrogenase (Decarboxylating); D005998:Glycine