scholarly journals Proximity of sulfhydryl groups in lens proteins. Excimer fluorescence of pyrene-labeled crystallins.

1990 ◽  
Vol 265 (24) ◽  
pp. 14277-14284
Author(s):  
A.C. Sen ◽  
B. Chakrabarti
Keyword(s):  
Sulfhydryl Groups ◽  
Lens Proteins ◽  
Excimer Fluorescence

Effect of the oxidation of sulfhydryl groups on lens proteins

1968 ◽  
Vol 7 (2) ◽  
pp. 276-IN36 ◽  
Author(s):  
M. Testa ◽  
C. Fiore ◽  
N. Bocci ◽  
S. Calabro
Keyword(s):  
Sulfhydryl Groups ◽  
Lens Proteins

Excimer fluorescence in lens proteins labelled with N(1-pyrene)maleimide

1989 ◽  
Vol 8 (5) ◽  
pp. 533-535
Author(s):  
Tatiana Putilina ◽  
Robert C. Augusteyn
Keyword(s):  
Lens Proteins ◽  
Excimer Fluorescence

HISTOCHEMICALLY DEMONSTRABLE SUCCINIC DEHYDROGENASE AND SULFHYDRYL GROUPS IN TISSUES OF ADRENALECTOMIZED RAT

1954 ◽  
Vol 16 (4) ◽  
pp. 315-322 ◽  
Author(s):  
Antti Telkkä ◽  
A. N Kuusisto ◽  
Kimmo K. Mustakallio
Keyword(s):  
Succinic Dehydrogenase ◽  
Sulfhydryl Groups

Iodoacetate inactivation of rape alcohol dehydrogenase

1980 ◽  
Vol 45 (5) ◽  
pp. 1601-1607 ◽  
Author(s):  
Marie Stiborová ◽  
Sylva Leblová
Keyword(s):  
Alcohol Dehydrogenase ◽  
Protein Molecule ◽  
Sulfhydryl Groups ◽  
Inactivation Rate ◽  
First Order ◽  
Ph Dependent ◽  
Kinetics Of

Iodoacetate inactivates rape alcohol dehydrogenase (ADH, EC 1.1.1.1). The inactivation rate follows the kinetics of the first order, is pH-dependent, and decreases below pH 7.5. Besides irreversible alkylation of the sulfhydryl groups of the enzyme iodoacetate also forms a reversible complex with rape ADH. The coenzyme (NAD) and its analogs (ATP, ADP, AMP) competitively protect the enzyme against alkylation; o-phenanthroline also protects the enzyme against alkylation yet noncompetitively with respect to iodoacetate. Imidazole and o-phenanthroline compete with one another for binding to the protein molecule of rape ADH. Whereas o-phenanthroline decreases the inactivation rate imidazole increases the rate of iodoacetate inactivation.

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