Literature DB >> 6714942

Amino-acid sequence and disulfide linkages of the anaphylatoxin, des-Arg omega-C5a, from porcine serum.

B Zimmermann, W Vogt.   

Abstract

The primary structure of the porcine complement-derived peptide, des-Arg omega-C5a, has been analysed. Des-Arg omega-C5a is the natural secondary product of the activation fragment of the fifth component of complement, C5a, and represents a classical anaphylatoxin. The elaborated amino-acid sequence confirms the structure of porcine C5a proposed earlier by Gerard and Hugli, with one exception. Further, by end-group determination and sequencing of the unreduced core of des-Arg omega-C5a the position of its three disulfide bridges has been determined, now allowing insight into the tertiary structure of des-Arg omega-C5a.

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Year:  1984        PMID: 6714942     DOI: 10.1515/bchm2.1984.365.1.151

Source DB:  PubMed          Journal:  Hoppe Seylers Z Physiol Chem        ISSN: 0018-4888


  3 in total

1.  Identification of receptor-binding residues in the inflammatory complement protein C5a by site-directed mutagenesis.

Authors:  K W Mollison; W Mandecki; E R Zuiderweg; L Fayer; T A Fey; R A Krause; R G Conway; L Miller; R P Edalji; M A Shallcross
Journal:  Proc Natl Acad Sci U S A       Date:  1989-01       Impact factor: 11.205

2.  Solution structure of a unique C5a semi-synthetic antagonist: implications in receptor binding.

Authors:  X Zhang; W Boyar; N Galakatos; N C Gonnella
Journal:  Protein Sci       Date:  1997-01       Impact factor: 6.725

3.  Cell-free synthesis of isotopically labelled peptide ligands for the functional characterization of G protein-coupled receptors.

Authors:  Lisa Joedicke; Raphael Trenker; Julian D Langer; Hartmut Michel; Julia Preu
Journal:  FEBS Open Bio       Date:  2015-12-29       Impact factor: 2.693

  3 in total

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