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Activation of a Latent Mushroom (Agaricus bisporus) Tyrosinase Isoform by Sodium Dodecyl Sulfate (SDS). Kinetic Properties of the SDS-Activated Isoform

This study reports the activation of a latent mushroom tyrosinase isoform by sodium dodecyl sulfate (SDS). The activation process of latent mushroom tyrosinase by SDS is characterized by the presence of a lag period (τ) prior to the attainment of a steady-state rate (V ss). This could be related to...

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Published in:Journal of agricultural and food chemistry 1999-09, Vol.47 (9), p.3518-3525
Main Authors: Espín, Juan Carlos, Wichers, Harry J
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Language:English
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cited_by cdi_FETCH-LOGICAL-a398t-8af005b137ee45db8c63f77bd0cb892fb4811f3d9f966ec069a80b7a3d1e5b553
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description This study reports the activation of a latent mushroom tyrosinase isoform by sodium dodecyl sulfate (SDS). The activation process of latent mushroom tyrosinase by SDS is characterized by the presence of a lag period (τ) prior to the attainment of a steady-state rate (V ss). This could be related to a slow conformational change of the latent enzyme to render the active isoform. The molecular size of the latent isoform was 67 kDa as determined by SDS−PAGE and western-blotting assays. This size did not change after activation by SDS. The molecular size of the protease-activated isoform was 43 kDa. τ and V ss displayed a sigmoidal relationship to the concentration of SDS, but τ was not dependent on o-diphenol or enzyme concentration. Increasing SDS concentrations decreased τ, but then lower V ss values were detected because of a possible excess of unfolding and subsequent denaturation of the protein. The same reaction mechanism operated in both SDS-activated and protease-activated tyrosinase isoforms despite their different kinetic features. A possible mechanism for the activation of this latent tyrosinase by SDS is proposed. Keywords: Agaricus; kinetics; latent; mushroom; SDS; tyrosinase.
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Kinetic Properties of the SDS-Activated Isoform</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>This study reports the activation of a latent mushroom tyrosinase isoform by sodium dodecyl sulfate (SDS). The activation process of latent mushroom tyrosinase by SDS is characterized by the presence of a lag period (τ) prior to the attainment of a steady-state rate (V ss). This could be related to a slow conformational change of the latent enzyme to render the active isoform. The molecular size of the latent isoform was 67 kDa as determined by SDS−PAGE and western-blotting assays. This size did not change after activation by SDS. The molecular size of the protease-activated isoform was 43 kDa. τ and V ss displayed a sigmoidal relationship to the concentration of SDS, but τ was not dependent on o-diphenol or enzyme concentration. 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Psychology</topic><topic>Instituut voor Agrotechnologisch Onderzoek</topic><topic>Isoenzymes - metabolism</topic><topic>Kinetics</topic><topic>Monophenol Monooxygenase - metabolism</topic><topic>Oxidoreductases</topic><topic>Sodium Dodecyl Sulfate - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Espín, Juan Carlos</creatorcontrib><creatorcontrib>Wichers, Harry J</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>NARCIS:Publications</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Espín, Juan Carlos</au><au>Wichers, Harry J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Activation of a Latent Mushroom (Agaricus bisporus) Tyrosinase Isoform by Sodium Dodecyl Sulfate (SDS). Kinetic Properties of the SDS-Activated Isoform</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>1999-09-01</date><risdate>1999</risdate><volume>47</volume><issue>9</issue><spage>3518</spage><epage>3525</epage><pages>3518-3525</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>This study reports the activation of a latent mushroom tyrosinase isoform by sodium dodecyl sulfate (SDS). The activation process of latent mushroom tyrosinase by SDS is characterized by the presence of a lag period (τ) prior to the attainment of a steady-state rate (V ss). This could be related to a slow conformational change of the latent enzyme to render the active isoform. The molecular size of the latent isoform was 67 kDa as determined by SDS−PAGE and western-blotting assays. This size did not change after activation by SDS. The molecular size of the protease-activated isoform was 43 kDa. τ and V ss displayed a sigmoidal relationship to the concentration of SDS, but τ was not dependent on o-diphenol or enzyme concentration. Increasing SDS concentrations decreased τ, but then lower V ss values were detected because of a possible excess of unfolding and subsequent denaturation of the protein. The same reaction mechanism operated in both SDS-activated and protease-activated tyrosinase isoforms despite their different kinetic features. A possible mechanism for the activation of this latent tyrosinase by SDS is proposed. Keywords: Agaricus; kinetics; latent; mushroom; SDS; tyrosinase.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>10552678</pmid><doi>10.1021/jf981275p</doi><tpages>8</tpages></addata></record>
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source American Chemical Society:Jisc Collections:American Chemical Society Read & Publish Agreement 2022-2024 (Reading list)
subjects Agaricales - enzymology
Agaricus - enzymology
Agrotechnological Research Institute
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Enzyme Activation
Enzymes and enzyme inhibitors
Food industries
Fruit and vegetable industries
Fundamental and applied biological sciences. Psychology
Instituut voor Agrotechnologisch Onderzoek
Isoenzymes - metabolism
Kinetics
Monophenol Monooxygenase - metabolism
Oxidoreductases
Sodium Dodecyl Sulfate - pharmacology
title Activation of a Latent Mushroom (Agaricus bisporus) Tyrosinase Isoform by Sodium Dodecyl Sulfate (SDS). Kinetic Properties of the SDS-Activated Isoform
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