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The double domain structure of rhodanese
Journal of Molecular Biology, 1975A 3 A electron density map of bovine liver rhodanese shows, in conjunction with gel electrophoresis experiments, that rhodanese consists of a single polypeptide chain with molecular weight of 32,000. The map reveals a very clear double domain structure of the molecule. The two domains are of equal size and have very similar conformations.
Bergsma, J. +5 more
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Thiosulphate sulphurtransferase (rhodanese) in cephalopoda
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1981Abstract 1. 1. The distribution of rhodanese activity in the homogenate and hyaloplasm obtained from gills, digestive gland and kidney of four cephalopods has been studied. 2. 2. The enzyme activity, which seems to be ubiquitous, is much higher in the octopods ( Octopus vulgaris Lam.
Claudio Agnisola +4 more
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Properties of Azotobacter vinelandii rhodanese.
Biochemistry and molecular biology international, 1993Rhodanese (thiosulfate: cyanide sulfurtransferase, E.C. 2.8.1.1) was purified from the nitrogen fixing organism Azotobacter vinelandii, and its amino acid composition was determined. The enzyme is a single polypeptide chain of M(r) 29,000 which showed an apparent pI of 4.7 and no presence of isoenzymes.
S, Pagani +3 more
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Cyanide Detoxifying Enzyme: Rhodanese
Current Biotechnology e, 2012Mayank Chaudhary, Reena Gupta
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Leber's optic atrophy and “rhodanese” activity
Medical Journal of Australia, 1988P J, Goadsby, R D, Fine
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[ERYTHROCYTIC RHODANESE IN CHILDHOOD].
La Pediatria, 1996M B, CANANI, F, REA
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