Side reaction of methionine with 4-vinylpyridine during acid hydrolysis of modified proteins.

doi:10.1016/0003-2697(80)90671-5

Paper

DOI: 10.1016/0003-2697(80)90671-5

Side reaction of methionine with 4-vinylpyridine during acid hydrolysis of modified proteins.

Published Dec 1, 1980 · J. Heukeshoven

Analytical biochemistry

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Abstract

Abstract hidden due to publisher request; this does not indicate any issues with the research. Click the full text link above to read the abstract and view the original source.

Study Snapshot

4-Vinylpyridine can cause a side reaction with methionine during acid hydrolysis of modified proteins, leading to the formation of a new ninhydrin-positive compound.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

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References

DOI: 10.1016/0003-2697(78)90382-2

The purification of peptides which contain methionine residues.

This study presents a novel method for isolating methionine-containing peptides from protein digests, enabling the purification of complex peptide mixtures and large proteins containing many methionine residues.

1978·19citations·J. Degen et al.·Analytical biochemistry

Analytical biochemistry

DOI: 10.1016/0003-2697(78)90061-1

Application of S-pyridylethylation of cysteine to the sequence analysis of proteins.

PTH-PECys can be used to accurately determine cysteine residues in proteins, with its unique UV spectrum aiding in enzymatic hydrolysis.

1978·14citations·A. Mak et al.·Analytical biochemistry

Analytical biochemistry

DOI: 10.1016/0003-2697(76)90509-1

Single analysis for cysteine, cystine, and tryptophan in proteins.

This study demonstrates a single-column method for analyzing cysteine, cystine, and tryptophan residues in proteins after acid hydrolysis, with minimal impact from tryptamine presence.

1976·30citations·A. Inglis et al.·Analytical biochemistry

Analytical biochemistry

DOI: 10.1002/JSFA.2740270302

Separation and characterisation of chymotryptic peptides from α- and β-purothionins of wheat†

Chymotryptic peptides from wheat's - and -purothionins reveal differences in their primary structures, with tyrosine likely being the thirteenth residue from the amino terminus.

1976·17citations·A. Mak et al.·Journal of the Science of Food and Agriculture

Journal of the Science of Food and Agriculture

DOI: 10.1177/004051757004001205

Cystine Content of Wool

The new method for quantitative determination of cysteine content in wool allows for routine analyses using ion-exchange chromatography and ultraviolet spectroscopy.

1970·48citations·M. Friedman et al.·Textile Research Journal

Textile Research Journal

DOI: 10.1016/s0021-9258(18)62930-8

The chromatographic determination of cystine and cysteine residues in proteins as s-beta-(4-pyridylethyl)cysteine.

This study demonstrates a method for quantitative determination of cysteine and cystine content in proteins and seed meals, using S-(4-pyridylethyl)-l-cysteine residues as a stable, acid-resistant derivative.

1970·437citations·M. Friedman et al.·The Journal of biological chemistry

The Journal of biological chemistry

DOI: 10.1016/0003-2697(70)90211-3

An internal standard for amino acid analyses: S-β-(4-pyridylethyl)-l-cysteine☆

PEC is a stable, internal standard for amino acid analyses, providing excellent results both before and after protein hydrolysis.

1970·122citations·J. F. Cavins et al.·Analytical Biochemistry

Analytical Biochemistry

DOI: 10.1016/s0021-9258(18)69921-1

The reaction of iodoacetate with methionine.

Iodoacetate readily reacts with methionine residues at neutral pH, potentially causing low methionine recoveries in protein analyses.

1959·172citations·Gundlach Hg et al.·The Journal of biological chemistry

The Journal of biological chemistry

Citations

DOI: 10.1016/j.chembiol.2014.09.002

Click chemistry in complex mixtures: bioorthogonal bioconjugation.

Recent developments in bioorthogonal chemistry have revolutionized selective chemical modification of biological molecules, advancing reaction rates, biocompatibility, and applications in drug development and fundamental biological research.

2014·606citations·Craig S Mckay et al.·Chemistry & biology

Chemistry & biology

DOI:

Development of new bioselective ligation reactions

A promising cysteine-selective scaffold, 3Garylpropiolonitrile (APN), was identified with remarkable selectivity, high reactivity, and potential for protein labeling.

2014·0citations·Oleksandr Koniev

DOI: 10.1021/bc400469d

Selective irreversible chemical tagging of cysteine with 3-arylpropiolonitriles.

3-arylpropiolonitriles (APN) show excellent chemoselectivity for cysteine, making them a promising method for bioconjugation applications.

2014·69citations·Oleksandr Koniev et al.·Bioconjugate chemistry

Bioconjugate chemistry

DOI: 10.1023/A:1012558530359

Application of the S-Pyridylethylation Reaction to the Elucidation of the Structures and Functions of Proteins

The S-pyridylethylation reaction effectively stabilizes cysteine residues in proteins, enabling their analysis and sequence determination in various applications.

2001·27citations·M. Friedman·Journal of Protein Chemistry

Journal of Protein Chemistry

DOI: 10.1111/J.1432-1033.1987.TB13466.X

Amino acid sequence similarity between malate dehydrogenases (NAD) and pea chloroplast malate dehydrogenase (NADP).

A common evolutionary origin for all malate dehydrogenases is suggested, with most peptides showing high homology with other enzymes, suggesting a common evolutionary origin for all malate dehydrogenases.

1987·23citations·K. Fickenscher et al.·European journal of biochemistry

European journal of biochemistry