منابع مشابه
Crystalline beef kidney rhodanese.
Although rhodanese activity occurs in many tissues (l-3), the enzyme had been obtained in crystalline form from beef liver only (4). Beef kidney rhodanese could not be crystallized by the same procedure (5). To extend the biochemical genetic comparison reported previously (5), however, it was desired to obtain the kidney enzyme in a very high state of purity. This paper reports the purification...
متن کاملReversible Folding of Rhodanese
For the first time completely reversible unfolding was achieved for guanidinium chloride-denatured rhodanese using a systematically defined protocol. These conditions included fl-mercaptoethanol, lauryl maltoside, and sodium thiosulfate. All components were required to get more than the previous best reactivation with lauryl maltoside of 17% (Tandon, S., and Horowitz, P. (1986) J. Biol. Chem. 2...
متن کاملThe rhodanese/Cdc25 phosphatase superfamily
Rhodanese domains are ubiquitous structural modules occurring in the three major evolutionary phyla. They are found as tandem repeats, with the C-terminal domain hosting the properly structured active-site Cys residue, as single domain proteins or in combination with distinct protein domains. An increasing number of reports indicate that rhodanese modules are versatile sulfur carriers that have...
متن کاملImproved Assay for Rhodanese in Thiobacillus spp.
Rhodanese (thiosulfate:cyanide sulfurtransferase; EC 2.8.1.1) catalyzes the conversion of thiosulfate and cyanide to thiocyanate and sulfite. Conventional rhodanese assays colorimetrically measure the formation of one or the other of the products. These assays suffer from the fact that there is significant nonbiological formation of these products in addition to the enzymatically catalyzed reac...
متن کاملAn expanded mechanism for rhodanese catalysis.
The kinetic behavior of rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1) was investigated at pH values from 5.0 to 10.8. The binding of thiosulfate was shown to be dependent upon a pK’ of 9.9, with the protonated enzyme binding the substrate much more strongly than the deprotonated form. An enzymic nucleophile displaces sulfite to form the sulfur-substituted enzyme. This reaction ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Acta Chemica Scandinavica
سال: 1953
ISSN: 0904-213X
DOI: 10.3891/acta.chem.scand.07-0238