Literature DB >> 3894052

The primary structure of two polypeptide chains from preparations of homeostatic thymus hormone (HTH alpha and HTH beta) entire-chain identities to two histones.

R Reichhart, H Jörnvall, M Carlquist, M Zeppezauer.   

Abstract

The primary structures of the 2 polypeptide chains (HTH alpha and HTH beta) of the homeostatic thymus hormone (HTH) were determined. The entire structures were found to be identical to those of histones H2A and H2B, respectively, without evidence for sub-types, proteolytic processings, or other peptide fragments. The results show that suggestions for new extranuclear and hormone-like histone functions apply to HTH preparations with intact protein chains of the H2 histones.

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Year:  1985        PMID: 3894052     DOI: 10.1016/0014-5793(85)80875-9

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


  2 in total

1.  Histones and basic polypeptides activate Ca2+/cation influx in various cell types.

Authors:  A Gamberucci; R Fulceri; P Marcolongo; W F Pralong; A Benedetti
Journal:  Biochem J       Date:  1998-04-15       Impact factor: 3.857

2.  Histone H4 stimulates glucose transport activity in rat skeletal muscle.

Authors:  L L Louters; E J Henriksen; C M Tipton
Journal:  Biochem J       Date:  1993-10-15       Impact factor: 3.857

  2 in total

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