Literature DB >> 6402383

Formation of the COOH-terminal amide group of thyrotropin-releasing-factor.

I Husain, S S Tate.   

Abstract

The precursors of peptide hormones that possess a COOH-terminal alpha-amide group contain a glycine residue following the amino acid which is amidated in the hormone. Less than Glu-His-Pro-Gly was synthesized as a putative precursor of thyroliberin. Bovine pituitary neurosecretory granules were shown to contain an amide group-forming activity associated with an Mr of about 62 000 protein(s) which converts the tetrapeptide to thyroliberin.

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Year:  1983        PMID: 6402383     DOI: 10.1016/0014-5793(83)80395-0

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  Evidence for high peptide alpha-amidating activity in the pancrease from neonatal rats.

Authors:  L Ouafik; P Giraud; P Salers; A Dutour; E Castanas; F Boudouresque; C Oliver
Journal:  Proc Natl Acad Sci U S A       Date:  1987-01       Impact factor: 11.205

2.  Glycine-directed peptide amidation: presence in rat brain of two enzymes that convert p-Glu-His-Pro-Gly-OH into p-Glu-His-Pro-NH2 (thyrotropin-releasing hormone).

Authors:  J S Kizer; W H Busby; C Cottle; W W Youngblood
Journal:  Proc Natl Acad Sci U S A       Date:  1984-05       Impact factor: 11.205

3.  Biosynthesis of thyrotropin releasing hormone in the skin of Xenopus laevis: partial sequence of the precursor deduced from cloned cDNA.

Authors:  K Richter; E Kawashima; R Egger; G Kreil
Journal:  EMBO J       Date:  1984-03       Impact factor: 11.598

  3 in total

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