Identification of chemical modification sites on metalloproteins by capillary electrophoresis

I. Jy Chang, Harry B. Gray, Michael Albin

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Capillary electrophoresis (CE) has been used to separate the peptides obtained from tryptic digestion of ruthenium-modified cytochrome c. The modified peptide was identified from a comparison of the elution profile and absorbance characteristics of the native and modified proteins. Automatic fraction collection on the CE instrument provides sufficient amounts of this modified peptide for amino acid sequencing. Capillary electrophoresis has also been used to monitor the modification reaction and to optimize the modification efficiency. The methodologies have been extended to myoglobin in order to monitor the modification of multiple surface sites.

Original languageEnglish
Pages (from-to)24-27
Number of pages4
JournalAnalytical Biochemistry
Volume212
Issue number1
DOIs
Publication statusPublished - 1993 Jan 1

Fingerprint

Metalloproteins
Capillary electrophoresis
Chemical modification
Capillary Electrophoresis
Peptides
Ruthenium
Myoglobin
Protein Sequence Analysis
Cytochromes c
Digestion
Amino Acids
Proteins

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Identification of chemical modification sites on metalloproteins by capillary electrophoresis. / Chang, I. Jy; Gray, Harry B.; Albin, Michael.

In: Analytical Biochemistry, Vol. 212, No. 1, 01.01.1993, p. 24-27.

Research output: Contribution to journalArticle

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