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

Miki Nakazawa; Katsushi Manabe

doi:10.1016/S0003-2697(05)80017-X

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 journal › Article › peer-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 language	English
Pages (from-to)	105-108
Number of pages	4
Journal	Analytical Biochemistry
Volume	206
Issue number	1
DOIs	https://doi.org/10.1016/S0003-2697(05)80017-X
Publication status	Published - Oct 1992
Externally published	Yes

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

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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.",

author = "Miki Nakazawa and Katsushi Manabe",

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AU - Nakazawa, Miki

AU - Manabe, Katsushi

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Y1 - 1992/10

N2 - 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.

AB - 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.

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DO - 10.1016/S0003-2697(05)80017-X

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AN - SCOPUS:0026802924

SN - 0003-2697

VL - 206

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JO - Analytical Biochemistry

JF - Analytical Biochemistry

IS - 1

ER -

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

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