Document Detail

Inactivation of human tyrosinase by cysteine. Protection by dopa and tyrosine.
MedLine Citation:
PMID:  6203305     Owner:  NLM     Status:  MEDLINE    
Human tyrosinase prepared from cultured melanoma cells is inactivated by 10 mM cysteine. The inactivation of the enzyme by cysteine is less pronounced in the presence of catalase and superoxide dismutase. Thus, oxygen radicals and/or hydrogen peroxide may contribute to the inactivation of human tyrosinase by cysteine. Dopa and/or tyrosine protects tyrosinase against inactivation by cysteine. The protection observed with tyrosine alone indicates that oxidation of substrate is not necessary for the protection. The effect of dopa and/or tyrosine is probably due to steric hindrance at the active site preventing the access of cysteine to the copper.
B Jergil; C Lindbladh; H Rorsman; E Rosengren
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Acta dermato-venereologica     Volume:  64     ISSN:  0001-5555     ISO Abbreviation:  Acta Derm. Venereol.     Publication Date:  1984  
Date Detail:
Created Date:  1984-07-09     Completed Date:  1984-07-09     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0370310     Medline TA:  Acta Derm Venereol     Country:  SWEDEN    
Other Details:
Languages:  eng     Pagination:  155-7     Citation Subset:  IM    
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MeSH Terms
Catalase / pharmacology
Catechol Oxidase / antagonists & inhibitors*
Cells, Cultured
Cysteine / pharmacology*
Levodopa / pharmacology*
Melanoma / enzymology*
Monophenol Monooxygenase / antagonists & inhibitors*,  isolation & purification
Superoxide Dismutase / pharmacology
Tyrosine / pharmacology*
Reg. No./Substance:
0/Levodopa; 52-90-4/Cysteine; 55520-40-6/Tyrosine; EC Oxidase; EC; EC Monooxygenase; EC Dismutase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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