Reversible inactivation of lysozyme due to N,O-peptidyl shift

Josefsson, Lars; Edman, Pehr

doi:10.1016/0006-3002(57)90535-8

Cited by 32 publications

(6 citation statements)

References 25 publications

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“…Available evidence (Josefsson and Edman. 1957;Martin et al, 1959;Narita, 1959;Smillie and Neurath, 1959) indicates that peptide bonds are not cleaved and extensive denaturation does not take place in formic acid solutions.…”

Section: Resultsmentioning

confidence: 99%

Physicochemical studies on the gelation of hen egg yolk; separation of gelling protein components from yolk plasma

Mahadevan¹,

Satyanarayana²,

Kumar³

1969

J. Agric. Food Chem.

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Section: Resultsmentioning

confidence: 99%

Physicochemical studies on the gelation of hen egg yolk; separation of gelling protein components from yolk plasma

Mahadevan¹,

Satyanarayana²,

Kumar³

1969

J. Agric. Food Chem.

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“…TNBS determinations showed no significant difference in free amino groups for both native and modified gelatins, demonstrating that there was no N to O acyl group formation between amino groups of the gelatin and the carboxylic group of the fatty acid. This result must be true, since the reaction took place in an acidic environment ( Josefsson and Edman 1957). Free amino group content of the esterified gelatin was 94.85% of that of the unmodified sample.…”

Section: Methodsmentioning

confidence: 92%

Chemical Modification of Pigskin Gelatin: Factors Affecting the Esterification of Gelatin with Fatty Acid

Djagny

Wang

2001

Journal of Food Science

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This study investigated the esterification of pigskin gelatin with fatty acid catalyzed by acid in aqueous medium. Factors affecting the esterification reaction B temperature, pH, water content, fatty acid concentration, fatty acid type and reaction time-were elucidated in the view of optimizing the reaction. Under the same experimental conditions, increase in fatty acid concentration permitted the determination of the maximum amount of fatty acid that could be esterified per unit weight of gelatin and demonstrated that not all the hydroxyl functional groups present in the gelatin could be blocked by the fatty acid chains.

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“…Since many proteins are unstable under these conditions (Josefsson and Edman, 1957;Smillie and Neurath, 1959), an aqueous solvent system would be preferable operationally.…”

Section: Resultsmentioning

confidence: 99%

“…In a previous note (Scoffone et al, 1966) we described the reaction of sulfenyl halides with proteins using glacial acetic acid or 99% formic acid as solvents. Since many proteins are unstable under these conditions (Josefsson and Edman, 1957; Smillie and Neurath, 1959), an aqueous solvent system would be preferable operationally.…”

Section: Resultsmentioning

confidence: 99%

Sulfenyl halides as modifying reagents for polypeptides and proteins. I. Modification of tryptophan residues

Scoffone¹,

Fontana²,

Rocchi³

1968

Biochemistry

219

101

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Sulfenyl halides have been found t o be specific, mild reagents for modification of tryptophan and cysteine residues of polypeptides and proteins in acidic media, such as acetic acid or formic acid. With hydrolysis-resistant halides, like 2-nitro-(NPS-C1) and 2,4-dinitrophenylsulfenyl chloride (DNPS-CI), the reaction can be carried out in aqueous solvents such as 30-50% acetic acid. Tryptophan is smoothly converted by reaction with sulfenyl halides into a derivative with a thioether function in the 2 position of the indole nucleus, and cysteine to an unsymmetrical disulfide. The high specificity of the reaction toward tryptophan and cysteine was established after quantitative recovery on the amino acid analyzer of the other amino acids, after 15-hr reaction with NPS-CI in acetic acid. As a further check, ribonuclease A, a protein containing neither tryptophan nor cysteine, was allowed to react with 20 equiv of NPS-CI in SOP;: acetic acid. The protein was recovered

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Reversible inactivation of lysozyme due to N,O-peptidyl shift

Cited by 32 publications

References 25 publications

Physicochemical studies on the gelation of hen egg yolk; separation of gelling protein components from yolk plasma

Physicochemical studies on the gelation of hen egg yolk; separation of gelling protein components from yolk plasma

Chemical Modification of Pigskin Gelatin: Factors Affecting the Esterification of Gelatin with Fatty Acid

Sulfenyl halides as modifying reagents for polypeptides and proteins. I. Modification of tryptophan residues

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