Literature DB >> 3766970

Hydrophobicity modulation as a tool for the purification of histidyl peptides.

M J Biscoglio de Jimenez Bonino, J G Fukushima, O Cascone.   

Abstract

A methodology is described for purification of histidyl peptides based on the changes in hydrophobicity induced by the specific and reversible modification of histidine residues by ethoxyformic anhydride. The mixture of modified peptides is subjected to HPLC; peptides containing modified histidines are detected at 242 nm, recovered, deethoxyformylated, and rechromatographed under the same conditions, then being detected at 220 nm. This procedure allows their isolation free from contaminants.

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Year:  1986        PMID: 3766970     DOI: 10.1016/0003-2697(86)90188-0

Source DB:  PubMed          Journal:  Anal Biochem        ISSN: 0003-2697            Impact factor:   3.365


  1 in total

1.  Single active-site histidine in D-xylose isomerase from Streptomyces violaceoruber. Identification by chemical derivatization and peptide mapping.

Authors:  W Vangrysperre; C Ampe; H Kersters-Hilderson; P Tempst
Journal:  Biochem J       Date:  1989-10-01       Impact factor: 3.857

  1 in total

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