Literature DB >> 2025283

The primary structure of human H-protein of the glycine cleavage system deduced by cDNA cloning.

K Fujiwara1, K Okamura-Ikeda, K Hayasaka, Y Motokawa.   

Abstract

A full-length cDNA encoding the human H-protein of the glycine cleavage system has been isolated from a lambda gt11 human fetal liver cDNA library. The cDNA insert was 1091 base pairs with an open reading frame of 519 base pairs which encoded a 125-amino acid mature human H-protein with a 48-amino acid presequence. Human H-protein is 97%, 86%, and 46% identical to the bovine, chicken, and pea H-protein, respectively.

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Year:  1991        PMID: 2025283     DOI: 10.1016/s0006-291x(05)80242-6

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  Cloning of the gene (gdcH) encoding H-protein, a component of the glycine decarboxylase complex of pea (Pisum sativum L.).

Authors:  D Macherel; J Bourguignon; R Douce
Journal:  Biochem J       Date:  1992-09-01       Impact factor: 3.857

2.  New nucleotide sequence data on the EMBL File Server.

Authors: 
Journal:  Nucleic Acids Res       Date:  1992-01-11       Impact factor: 16.971

  2 in total

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