Peptic peptide of thiolsubtilisin. Analytical evidence for the chemical transformation of the essential serine-221 to cysteine-221

L. Polgár, Mihály Sajgó

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Abstract

Direct evidence is offered to show that the active site Ser-221 of subtilisin is transformed into a cysteine residue in the chemical procedure previously elaborated for the preparation of thiolsubtilisin. Thiolsubtilisin was digested with pepsin and the hydrolyzate was applied to an agarose-mercurial column. After elution with 2-mercaptoethanol a single tetrapeptide was obtained. Dansyl-Edman degradation showed that the SH-peptide conformed to the amino acid sequence around the active site Ser-221 of subtilisin. A simple single-step procedure for isolation of SH-peptides is also described.

Original languageEnglish
Pages (from-to)351-354
Number of pages4
JournalBBA - Protein Structure
Volume667
Issue number2
DOIs
Publication statusPublished - Feb 27 1981

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Keywords

  • Affinity chromatography
  • Subtilisin
  • Sulfhydryl peptide
  • Thiolsubtilisin

ASJC Scopus subject areas

  • Medicine(all)

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