Literature DB >> 8401334

Determination of halfcystine in proteins as cysteine from reducing hydrolyzates.

L Sottrup-Jensen1.   

Abstract

The separation of cysteine from proline using a variant of the classical cation exchange system for amino acid analysis is described. From reducing hydrolyzates (6 M HCl/0.1% phenol/5% thioglycollic acid, 18 h, 110 degrees C) the halfcystine content of proteins can be accurately determined as cysteine. The system is useful for routine determination of the composition of proteins from a single type of hydrolyzate.

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Year:  1993        PMID： 8401334

Source DB:  PubMed          Journal:  Biochem Mol Biol Int        ISSN： 1039-9712


  3 in total

1.  Revisiting the structure of the Vps10 domain of human sortilin and its interaction with neurotensin.

Authors:  Esben M Quistgaard; Morten K Grøftehauge; Peder Madsen; Lone T Pallesen; Brian Christensen; Esben S Sørensen; Poul Nissen; Claus M Petersen; Søren S Thirup
Journal:  Protein Sci       Date:  2014-07-22       Impact factor: 6.725

2.  Substrate specificity of the metalloproteinase pregnancy-associated plasma protein-A (PAPP-A) assessed by mutagenesis and analysis of synthetic peptides: substrate residues distant from the scissile bond are critical for proteolysis.

Authors:  Lisbeth S Laursen; Michael T Overgaard; Claus G Nielsen; Henning B Boldt; Kathrin H Hopmann; Cheryl A Conover; Lars Sottrup-Jensen; Linda C Giudice; Claus Oxvig
Journal:  Biochem J       Date:  2002-10-01       Impact factor: 3.857

3.  Characterization of two serpins from bovine plasma and milk.

Authors:  S Christensen; L Sottrup-Jensen
Journal:  Biochem J       Date:  1994-10-15       Impact factor: 3.857
  3 in total

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