@ARTICLE{Kachurin19981183,
author={Kachurin, A.M. and Protasenya, S.V. and Shabalin, K.A. and Isaev-Ivanov, V.V. and Golubev, A.M. and Neustroev, K.N.},
title={Tryptophan residues in α-galactosidase from Trichoderma reesei},
journal={Biochemistry (Moscow)},
year={1998},
volume={63},
number={10},
pages={1183-1190},
note={cited By 1},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032175116&partnerID=40&md5=27f87fcfbac7ed8407da523139b06a4a},
affiliation={St. Petersburg Konstantinov N.P.I., Orlova rosbcha, Gatchina 188351, Russian Federation},
abstract={Tryptophan residues in α-galactosidase were modified with bromosuccinimide. The fact that galactose, a specific inhibitor of α-galactosidase, does not prevent this modification demonstrates that tryptophan residues are not located in galactose binding sites. Analysis of the inactivation kinetics revealed two groups of Trp residues (8.5 and 7.5 residues) with different accessibility for N-bromosuccinimide. We studied specific quenching of α-galactosidase fluorescence resulting from modification of an sulfhydryl group in the active site of the enzyme with Hg2+ and Ag+ ions. The specific quenching is due to conformational changes of the enzyme. Forster's radii were determined for various protein-chromophore complexes. Dynamic quenching of α-galactosidase fluorescence was investigated. To describe abnormal dynamic quenching in α-galactosidase, a modification of the Stern-Volmer equation is suggested.},
author_keywords={α-galactosidase;  Enzyme active site;  Fluorescence spectroscopy;  Sulfhydryl group;  Trichoderma reesei},
correspondence_address1={Neustroev, K.N.; St. Petersburg Konstantinov N.P.I., Orlova rosbcha, Gatchina 188351, Russian Federation; email: neustk@omrb.pnpi.spb.ru},
issn={00062979},
coden={BIORA},
pubmed_id={9864453},
language={English},
abbrev_source_title={Biochemistry Moscow},
document_type={Article},
source={Scopus},
}

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The fact that galactose, a specific inhibitor of α-galactosidase, does not prevent this modification demonstrates that tryptophan residues are not located in galactose binding sites. Analysis of the inactivation kinetics revealed two groups of Trp residues (8.5 and 7.5 residues) with different accessibility for N-bromosuccinimide. We studied specific quenching of α-galactosidase fluorescence resulting from modification of an sulfhydryl group in the active site of the enzyme with Hg2+ and Ag+ ions. The specific quenching is due to conformational changes of the enzyme. Forster's radii were determined for various protein-chromophore complexes. Dynamic quenching of α-galactosidase fluorescence was investigated. To describe abnormal dynamic quenching in α-galactosidase, a modification of the Stern-Volmer equation is suggested.","author_keywords":"α-galactosidase; Enzyme active site; Fluorescence spectroscopy; Sulfhydryl group; Trichoderma reesei","correspondence_address1":"Neustroev, K.N.; St. Petersburg Konstantinov N.P.I., Orlova rosbcha, Gatchina 188351, Russian Federation; email: neustk@omrb.pnpi.spb.ru","issn":"00062979","coden":"BIORA","pubmed_id":"9864453","language":"English","abbrev_source_title":"Biochemistry Moscow","document_type":"Article","source":"Scopus","bibtex":"@ARTICLE{Kachurin19981183,\r\nauthor={Kachurin, A.M. and Protasenya, S.V. and Shabalin, K.A. and Isaev-Ivanov, V.V. and Golubev, A.M. and Neustroev, K.N.},\r\ntitle={Tryptophan residues in α-galactosidase from Trichoderma reesei},\r\njournal={Biochemistry (Moscow)},\r\nyear={1998},\r\nvolume={63},\r\nnumber={10},\r\npages={1183-1190},\r\nnote={cited By 1},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032175116&partnerID=40&md5=27f87fcfbac7ed8407da523139b06a4a},\r\naffiliation={St. Petersburg Konstantinov N.P.I., Orlova rosbcha, Gatchina 188351, Russian Federation},\r\nabstract={Tryptophan residues in α-galactosidase were modified with bromosuccinimide. The fact that galactose, a specific inhibitor of α-galactosidase, does not prevent this modification demonstrates that tryptophan residues are not located in galactose binding sites. Analysis of the inactivation kinetics revealed two groups of Trp residues (8.5 and 7.5 residues) with different accessibility for N-bromosuccinimide. We studied specific quenching of α-galactosidase fluorescence resulting from modification of an sulfhydryl group in the active site of the enzyme with Hg2+ and Ag+ ions. The specific quenching is due to conformational changes of the enzyme. Forster's radii were determined for various protein-chromophore complexes. Dynamic quenching of α-galactosidase fluorescence was investigated. 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