The thiol groups of aldolase
نویسندگان
چکیده
منابع مشابه
The reactivity of thiol groups and the subunit structure of aldolase.
1. Seven unique carboxymethylcysteine-containing peptides have been isolated from tryptic digests of rabbit muscle aldolase carboxymethylated with iodo[2-(14)C]acetic acid in 8m-urea. These peptides have been characterized by amino acid and end-group analysis and their location within the cyanogen bromide cleavage fragments of the enzyme has been determined. 2. Reaction of native aldolase with ...
متن کاملThe thiol groups of fumarase.
Several reagents have been employed to determine the role of the thiol groups in fumarase. The nature of the reaction of these reagents indicates that the thiol groups are not associated with active site structures but are buried in a hydrophobic environment in the interior of the enzyme. Several observations are in accord with this view. The rate of reaction of the thiol groups is much slower ...
متن کاملPathways of peroxynitrite oxidation of thiol groups.
Peroxynitrite mediates the oxidation of the thiol group of both cysteine and glutathione. This process is associated with oxygen consumption. At acidic pH and a cysteine/peroxynitrite molar ratio of < or = 1.2, there was a single fast phase of oxygen consumption, which increased with increasing concentrations of both cysteine and oxygen. At higher molar ratios the profile of oxygen consumption ...
متن کاملThe reactivity of the thiol groups of calf thymus deoxyribonucleohistone.
The reactivities of the two cysteine thiol groups of calf thymus F3 histone were investigated using 5,5'-dithiobis-[2- nitrobenzoic acid], (DTNB). In isolated histone, both thiol groups were available for reaction. However, analysis of reaction profiles of native deoxyribonucleohistone, (DNH), in various solvent conditions, together with gel electrophoresis studies of DNH modified with DTNB, sh...
متن کاملRole of the essential thiol groups of yeast alcohol dehydrogenase.
1. Yeast alcohol dehydrogenase inactivated by reaction with iodoacetamide retains 85% of the original NADH-binding capacity as measured under conditions of saturating coenzyme concentration. 2. The dissociation constant of the enzyme-NADH complex is unaffected by inactivation of the enzyme with iodoacetamide, and the affinity of the enzyme for NAD(+) and pyridine-3-aldehyde-adenine dinucleotide...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1970
ISSN: 0306-3283
DOI: 10.1042/bj1170049pb