1981
DOI: 10.1016/s0021-9258(19)70135-5
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The single tryptophan residue of human placental lactogen. Effects of modification and cleavage on biologic activity and protein conformation.

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Cited by 6 publications
(2 citation statements)
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“…For example, Trp can be oxidized to N -formyl kynurenine (NFK) and kynurenine and sensitize the reduction of peptide and/or disulfide bonds, forming thiyl radicals and thiolate. , The latter process requires photoinduced electron or H atom transfer between Trp and the disulfide bond. Modification of Trp residues in proteins has resulted in conformational changes and loss of biologic activity and presents a major concern for the production and formulation of biopharmaceuticals. Moreover, kynurenines are efficient photosensitizers, inferring that Trp oxidation can lead to additional photosensitivity of a protein formulation …”
mentioning
confidence: 99%
“…For example, Trp can be oxidized to N -formyl kynurenine (NFK) and kynurenine and sensitize the reduction of peptide and/or disulfide bonds, forming thiyl radicals and thiolate. , The latter process requires photoinduced electron or H atom transfer between Trp and the disulfide bond. Modification of Trp residues in proteins has resulted in conformational changes and loss of biologic activity and presents a major concern for the production and formulation of biopharmaceuticals. Moreover, kynurenines are efficient photosensitizers, inferring that Trp oxidation can lead to additional photosensitivity of a protein formulation …”
mentioning
confidence: 99%
“…Single amino acid changes in proteins have been studied through chemical modification or amino acid substitution to identify the residues responsible for binding activity and structure changes of proteins. It has been shown that modification of a single amino acid residue can affect the stability, structure, and activity of proteins. For instance, chemical oxidation of a single Trp in human placental lactogen resulted in conformational changes and reduced lactogenic activity . A single Trp-139 in the thermostable d -amino acid transaminase was critical for its activity, as proved by site-directed mutagenesis .…”
mentioning
confidence: 99%