PHOTOCHEMICAL‐LIKE DESTRUCTION OF TRYPTOPHAN IN SERUM ALBUMINS INDUCED BY ENZYME‐GENERATED TRIPLET SPECIES

Abstract —Human and bovine serum albumin quench enzyme‐generated acetone phosphorescence (Ksv=ca. 104M1). Concomitantly, these proteins are altered as shown by diminished tryptophan absorption at 280 nm, appearance of products of the formylkynurenine type (max=ca. 320 nm) and disappearance of trypto...

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Publicado:	1984
Materias:	acetone bovine serum albumin horseradish peroxidase serum albumin tryptophan animal article cattle human luminescence metabolism methodology spectrofluorometry Acetone Animal Cattle Horseradish Peroxidase Human Luminescence Serum Albumin Serum Albumin, Bovine Spectrometry, Fluorescence Support, Non-U.S. Gov't Tryptophan
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00318655_v40_n5_p565_Rivas http://hdl.handle.net/20.500.12110/paper_00318655_v40_n5_p565_Rivas
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_00318655_v40_n5_p565_Rivas
record_format	dspace
spelling	paper:paper_00318655_v40_n5_p565_Rivas2023-06-08T14:57:14Z PHOTOCHEMICAL‐LIKE DESTRUCTION OF TRYPTOPHAN IN SERUM ALBUMINS INDUCED BY ENZYME‐GENERATED TRIPLET SPECIES acetone bovine serum albumin horseradish peroxidase serum albumin tryptophan animal article cattle human luminescence metabolism methodology spectrofluorometry Acetone Animal Cattle Horseradish Peroxidase Human Luminescence Serum Albumin Serum Albumin, Bovine Spectrometry, Fluorescence Support, Non-U.S. Gov't Tryptophan Abstract —Human and bovine serum albumin quench enzyme‐generated acetone phosphorescence (Ksv=ca. 104M1). Concomitantly, these proteins are altered as shown by diminished tryptophan absorption at 280 nm, appearance of products of the formylkynurenine type (max=ca. 320 nm) and disappearance of tryptophan fluorescence. These alterations—which are similar to those induced photochemically—were also observed with serum albumins exposed to enzyme‐generated triplet acetaldehyde. On the other hand, triplet acetone generated by the thermolysis of tetramethyldioxetane failed to induce alterations. Presumably energy transfer occurs from the enzyme‐generated triplet species to tryptophan group(s) in the serum albumin associated with the acting enzyme. The detailed mechanism is, however, not yet understood. Copyright © 1984, Wiley Blackwell. All rights reserved 1984 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00318655_v40_n5_p565_Rivas http://hdl.handle.net/20.500.12110/paper_00318655_v40_n5_p565_Rivas
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	acetone bovine serum albumin horseradish peroxidase serum albumin tryptophan animal article cattle human luminescence metabolism methodology spectrofluorometry Acetone Animal Cattle Horseradish Peroxidase Human Luminescence Serum Albumin Serum Albumin, Bovine Spectrometry, Fluorescence Support, Non-U.S. Gov't Tryptophan
spellingShingle	acetone bovine serum albumin horseradish peroxidase serum albumin tryptophan animal article cattle human luminescence metabolism methodology spectrofluorometry Acetone Animal Cattle Horseradish Peroxidase Human Luminescence Serum Albumin Serum Albumin, Bovine Spectrometry, Fluorescence Support, Non-U.S. Gov't Tryptophan PHOTOCHEMICAL‐LIKE DESTRUCTION OF TRYPTOPHAN IN SERUM ALBUMINS INDUCED BY ENZYME‐GENERATED TRIPLET SPECIES
topic_facet	acetone bovine serum albumin horseradish peroxidase serum albumin tryptophan animal article cattle human luminescence metabolism methodology spectrofluorometry Acetone Animal Cattle Horseradish Peroxidase Human Luminescence Serum Albumin Serum Albumin, Bovine Spectrometry, Fluorescence Support, Non-U.S. Gov't Tryptophan
description	Abstract —Human and bovine serum albumin quench enzyme‐generated acetone phosphorescence (Ksv=ca. 104M1). Concomitantly, these proteins are altered as shown by diminished tryptophan absorption at 280 nm, appearance of products of the formylkynurenine type (max=ca. 320 nm) and disappearance of tryptophan fluorescence. These alterations—which are similar to those induced photochemically—were also observed with serum albumins exposed to enzyme‐generated triplet acetaldehyde. On the other hand, triplet acetone generated by the thermolysis of tetramethyldioxetane failed to induce alterations. Presumably energy transfer occurs from the enzyme‐generated triplet species to tryptophan group(s) in the serum albumin associated with the acting enzyme. The detailed mechanism is, however, not yet understood. Copyright © 1984, Wiley Blackwell. All rights reserved
title	PHOTOCHEMICAL‐LIKE DESTRUCTION OF TRYPTOPHAN IN SERUM ALBUMINS INDUCED BY ENZYME‐GENERATED TRIPLET SPECIES
title_short	PHOTOCHEMICAL‐LIKE DESTRUCTION OF TRYPTOPHAN IN SERUM ALBUMINS INDUCED BY ENZYME‐GENERATED TRIPLET SPECIES
title_full	PHOTOCHEMICAL‐LIKE DESTRUCTION OF TRYPTOPHAN IN SERUM ALBUMINS INDUCED BY ENZYME‐GENERATED TRIPLET SPECIES
title_fullStr	PHOTOCHEMICAL‐LIKE DESTRUCTION OF TRYPTOPHAN IN SERUM ALBUMINS INDUCED BY ENZYME‐GENERATED TRIPLET SPECIES
title_full_unstemmed	PHOTOCHEMICAL‐LIKE DESTRUCTION OF TRYPTOPHAN IN SERUM ALBUMINS INDUCED BY ENZYME‐GENERATED TRIPLET SPECIES
title_sort	photochemical‐like destruction of tryptophan in serum albumins induced by enzyme‐generated triplet species
publishDate	1984
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00318655_v40_n5_p565_Rivas http://hdl.handle.net/20.500.12110/paper_00318655_v40_n5_p565_Rivas
_version_	1768543598702231552

PHOTOCHEMICAL‐LIKE DESTRUCTION OF TRYPTOPHAN IN SERUM ALBUMINS INDUCED BY ENZYME‐GENERATED TRIPLET SPECIES

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