Book ChapterDOI
[35] Detection of peptides by chemical methods
TLDR
This chapter describes various chemical methods used in the detection of peptides and the reaction of ninhydrin with peptides, which is a complex reaction at α- and ɛ-amino groups and hydrolysis.Abstract:
Publisher Summary This chapter describes various chemical methods used in the detection of peptides The reactions with ninhydrin and with the Folin-Lowry reagent are both used for the detection and estimation of peptides in solution The reaction of ninhydrin with peptides is complex because, in addition to reaction at α- and ɛ-amino groups, hydrolysis may also occur The rates of these processes are a function of the structure of the peptide The variability of color yield is decreased and the overall sensitivity of the procedure is increased when the peptide is first subjected to hydrolysis Three major chemical methods discussed are (1) ninhydrin reagent, (2) alkaline hydrolysis, and (3) ninhydrin reaction Ninhydrin reagent involves three preparation steps, namely––the methyl cellosolve, buffer solution 4M, pH 5 , and preparation and storage of reagent In alkaline hydrolysis, the reaction is performed in polypropylene test tubes and the samples to be analyzed are carefully pipetted into the bottoms of the tubes The procedure of the ninhydrin reaction is also discussedread more
Citations
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The size and detergent binding of membrane proteins.
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References
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Journal Article
Protein Measurement with the Folin Phenol Reagent
TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
Journal ArticleDOI
A modified ninhydrin reagent for the photometric determination of amino acids and related compounds
Stanford Moore,William H. Stein +1 more
TL;DR: A modified ninhydrin reagent for the photometric determination of amino acids and related compounds and its application in drug discovery is described.
Journal ArticleDOI
Peptides obtained by tryptic hydrolysis of performic acid-oxidized ribonuclease.
TL;DR: In the present study, the chemical structure of ribonuclease has been investigated by the use of trypsin as a reagent for the hydrolysis of specific peptide bonds in the oxidized protein, and the resulting peptides have been separated and analyzed by ion exchange chromatography.
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