The primary structure of human gamma-glutamyl transpeptidase

Sakamuro Daitoku, Yamazoe Mitsuyoshi, Matsuda Yukihiko, Kangawa Kenji, Taniguchi Naoyuki, Matsuo Hisayuki, Yoshikawa Hiroshi, Ogasawara Naotake

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


A cDNA hybridizable to that of rat γ-glutamyl transpeptidase (GGT) was cloned from a cDNA library of human fetal liver. The insert of the cDNA clone contained 1866 bp consisting of an open reading frame (ORF) of 1709 bp (569 amino acids (aa), N-terminal portion truncated) and a 135-bp 3'-untranslated region followed by a polyadenylated tail. In parallel, amino acid sequences of N-terminal portions of heavy and light chains of a purified human GGT were determined. Two stretches of amino acid sequences identical to the N-terminal sequences of heavy and light chains were found in the ORF. We therefore concluded that the clone is a cDNA for human GGT. From the amino acid sequence deduced from cDNA, the heavy and the light chains of the purified enzyme are estimated to be composed of 351 aa (Mr 38336) and of 189 aa (Mr 20000), respectively. The heavy chain is preceded by a signal peptide of at least 29 aa presumed to be cleaved by bromelain treatment. Six putative N-glycosylation sites are present in the heavy subunit region and one in the light subunit region. Primary structure and hydrophobicity profile are closely similar to those of rat GGT.

Original languageEnglish (US)
Pages (from-to)1-9
Number of pages9
Issue number1
StatePublished - Dec 15 1988
Externally publishedYes


  • Recombinant DNA
  • amino acid sequence
  • cDNA
  • human fetal liver
  • human kidney
  • nucleotide sequence
  • rat enzyme

ASJC Scopus subject areas

  • Genetics


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