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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Autores principales: Rivas, E.I., Paladini, A., Jr, Cilento, G.
Formato: JOUR
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00318655_v40_n5_p565_Rivas
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spelling todo:paper_00318655_v40_n5_p565_Rivas2023-10-03T14:41:30Z PHOTOCHEMICAL‐LIKE DESTRUCTION OF TRYPTOPHAN IN SERUM ALBUMINS INDUCED BY ENZYME‐GENERATED TRIPLET SPECIES Rivas, E.I. Paladini, A., Jr Cilento, G. 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 JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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
Rivas, E.I.
Paladini, A., Jr
Cilento, G.
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
format JOUR
author Rivas, E.I.
Paladini, A., Jr
Cilento, G.
author_facet Rivas, E.I.
Paladini, A., Jr
Cilento, G.
author_sort Rivas, E.I.
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
url http://hdl.handle.net/20.500.12110/paper_00318655_v40_n5_p565_Rivas
work_keys_str_mv AT rivasei photochemicallikedestructionoftryptophaninserumalbuminsinducedbyenzymegeneratedtripletspecies
AT paladiniajr photochemicallikedestructionoftryptophaninserumalbuminsinducedbyenzymegeneratedtripletspecies
AT cilentog photochemicallikedestructionoftryptophaninserumalbuminsinducedbyenzymegeneratedtripletspecies
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