The direct hydrolysis of proteins containing tryptophanon polyvinylidene difluoride membranes by mercaptoethanesulfonic acid in the vapor phase

Miki Nakazawa, Katsushi Manabe

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

A procedure for the amino acid analysis of polypeptides that contain tryptophan on polyvinylidene difluoride membranes is described. Lysozyme, carbonic anhydrase, phytochrome, and ovalbumin were tested. The protein, which was separated from others by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, was blotted from the gel onto a polyvinylidene difluoride membrane and directly hydrolyzed by 3 n aptoethanesulfonic acid vapor in a vacuum at 176°C for 25 min. The hydrolysate was extracted with 0.1 n HCl and 30% methanol and used for amino acid analysis. The tested proteins were adequately hydrolyzed, and the recovery of tryptophan was very efficient.

Original languageEnglish
Pages (from-to)105-108
Number of pages4
JournalAnalytical Biochemistry
Volume206
Issue number1
DOIs
Publication statusPublished - Oct 1992
Externally publishedYes

Field of Science

  • 1.6 Biological sciences
  • 1.4 Chemical sciences

Publication Type

  • 1.1. Scientific article indexed in Web of Science and/or Scopus database

Fingerprint

Dive into the research topics of 'The direct hydrolysis of proteins containing tryptophanon polyvinylidene difluoride membranes by mercaptoethanesulfonic acid in the vapor phase'. Together they form a unique fingerprint.

Cite this