Disulfide reduction and sulfhydryl oxidation by microbial enzyme. II. Screening for the producer of thiol-disulfide interchange enzyme in yeasts and culture conditions for the enzyme from Candida claussenii.
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Purification and properties of an enzyme from beef liver which catalyzes sulfhydryl-disulfide interchange in proteins.
An enzyme which catalyzes sulfhydryl-disulfide interchange in proteins containing “incorrect” disulfide bonds has been isolated from beef liver microsomes. The purified form of this enzyme shows two bands upon electrophoresis in starch gels and polyacrylamide gels. The proteins represented by these bands are considered to be variants of the same protein because both are enzymically active after...
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Thiol/disulfide exchange between rabbit muscle phosphofructokinase and glutathione. Kinetics and thermodynamics of enzyme oxidation.
Reversible thiol/disulfide exchange equilibria between rabbit muscle phosphofructokinase and glutathione redox buffers results in a dependence of the activity of the enzyme on the thiol to disulfide ratio of the redox buffer (Gilbert, H. F. (1982) J. Biol. Chem. 257, 12086-12091). The transition between fully reduced (active) and fully oxidized (inactive) enzyme is half complete at a [GSH]/[GSS...
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In addition, it has been detected in most rat tissues studied. Its pH optimum is 8.2 and the equilibrium constant for the reaction is near unity at pH 6.9 and 25’. Michaelis constants for reduced glutathione and CoASSG are 3.3 x 10-4?d and 4.5 x 10-5b& respectively. The molecular weight of the enzyme, determined by gel filtration, is approximately 12,000. Several unsymmetrical disulfides contai...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1975
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.39.1411