Cloning of cDNA encoding human H-protein, a constituent of the glycine cleavage system

Koichi Hiraga, Shigeo Kure, Masayuki Yamamoto, Yoshihisa Ishiguro, Tamio Suzuki

研究成果: Article査読

8 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)758-762
ページ数5
ジャーナルBiochemical and biophysical research communications
151
2
DOI
出版ステータスPublished - 1988 3 15
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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