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PMID: 7106109 Published · ppublish English Journal Article

A rapid method for acid hydrolysis of protein with a mixture of trifluoroacetic acid and hydrochloric acid.

European journal of biochemistry ·Vol. 124 ·No. 3 ·1982-06-00 ·Pages 585-8

Tsugita A, Scheffler JJ

Abstract

Proteins have regions which resist hydrolysis with mineral acid. The presence of a strong organic acid was found to be efficient for hydrolysis of a hydrophobic peptide bond. The proposed condition, a 2:1 (by vol.) mixture of concentrated hydrochloric acid and trifluoroacetic acid at 166 degrees C for 25 min was observed to be equivalent to the conventional conditions (6 M HCl at 110 degrees C for more than 24 h) without significant decomposition of amino acids. The method was shown to be superior to the conventional conditions, especially for hydrophobic proteins. The present method destroys tryptophan, as the conventional acid hydrolysis does.

MeSH Terms
Acetates Acetic Acid Amino Acids/analysis Fluoroacetates Formates Hydrochloric Acid Hydrolysis Methods Peptide Fragments Propionates Proteins Trifluoroacetic Acid
Chemicals
Acetates Amino Acids Fluoroacetates Formates Peptide Fragments Propionates Proteins formic acid Trifluoroacetic Acid Acetic Acid Hydrochloric Acid
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Tsugita A
Scheffler J J
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1982-06-00
Pages
585-8
Language
English
Region
England
NLM ID
0107600
Subset
IM
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