Enzymatic Conversion of Cyanide to Thiocyanate

Himwich, Williamina A.; Saunders, Jack P.

doi:10.1152/ajplegacy.1948.153.2.348

Cited by 145 publications

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“…Lang (1933a) showed the presence of heat labile enzyme of optimum temperature of 38 o C in a rat liver. Himwich and Saunders (1948), working on bovine liver rhodanese, obtained an optimum temperature between 38 o C and 40 o C. Sorbo (1953aSorbo ( , 1953b also reported an optimum temperature of 50 o C from bovine liver. Chew and Boey (1972) obtained an optimum temperature between 57 o C and 59 o C from the rhodanese of tapioca leaves.…”

Section: Discussionmentioning

confidence: 96%

“…2.8.1.1) catalyses the formation of thiocyanate from free cyanide and a sulphur donor. It has been studied from variety of sources, which include bacteria, yeast, plants, and animals (Cosby and Summer, 1945;Himwich and Saunders, 1948;Sorbo, 1951;Jarabak and Westley, 1974;Anosike and Ugochukwu, 1981;Lee et al, 1995). It is a heat labile enzyme with an optimum pH of 8.0 and an average molecular weight of about 37,000.…”

Section: Introductionmentioning

confidence: 99%

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Presence of Rhodanese in the Cytosolic Fraction of the Fruit Bat (Eidolon helvum) Liver

Agboola¹,

Okonji²

2004

BMB Reports

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Rhodanese was isolated and purified from the cytosolic fraction of liver tissue homogenate of the fruit bat, Eidolon helvum, by using ammonium sulphate precipitation and CM-Sephadex C-50 ion exchange chromatography. The specific activity was increased 130-fold with a 53% recovery. The K m values for KCN and Na 2 S 2 O 3 as substrates were 13.5 ± 2.2 mM and 19.5 ± 0.7 mM, respectively. The apparent molecular weight was estimated by gel filtration on a Sephadex G-100 column to be 36,000 Da. The optimal activity was found at a high pH (pH 9.0) and the temperature optimum was

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Section: Discussionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

Presence of Rhodanese in the Cytosolic Fraction of the Fruit Bat (Eidolon helvum) Liver

Agboola¹,

Okonji²

2004

BMB Reports

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“…It is noteworthy that in addition to the pigeon, some other species also have the highest activity of rhodanese in organs other than the liver. For example the highest activity of this enzyme in dogs was found in the adrenal glands [12]. In several species the digestive system has been shown to contain higher activities of rhodanese than the liver [2,5,6].…”

Section: Discussionmentioning

confidence: 99%

Tissue and intracellular distribution of rhodanese and mercaptopyruvate sulphurtransferase in ruminants and birds

2001

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-Cyanide detoxification is catalysed by two enzymes: rhodanese [thiosulphate: cyanide sulphurtransferase, E.C. 2.8.1.1], and 3-mercaptopyruvate sulphurtransferase [3-MST, EC. 2.8.1.2]. In the present work, the activity of the two enzymes in the crude extracts of different tissues and in the mitochondrial and cytosolic fractions of tissues from some ruminants (camels, cattle and sheep) and birds (chickens and pigeons) have been compared. Rhodanese activity was almost exclusively present in the mitochondrial fraction. In ruminants and chickens the highest activity of rhodanese was found in the liver, followed by the kidney. In pigeons, however, the enzyme activity was the highest in the kidneys. In camels' tissues, the rhodanese activity was significantly (P < 0.05) lower than in cattle or sheep, and the enzyme activities in the two latter species were similar. The activity of 3-MST in the crude extract of tissues from camels was similar to that in sheep, but higher than that in cattle. The enzyme activity was equally distributed between the mitochondrial and cytosolic fractions in the liver and kidneys of camels, cattle and sheep. Chez les ruminants et les poulets, la plus forte activité du rhodanese a été trouvée dans le foie, suivi par le rein. Cependant, chez le pigeon, l'activité enzymatique la plus forte a été détectée dans le rein. Dans les tissus du chameau, l'activité du rhodanese était significativement (P < 0,05) plus faible que chez le bovin et le mouton, et les activités enzymatiques chez ces deux dernières espèces

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“…Urinary excretion may not reflect circulating levels because in part thiocyanate is formed in vivo from cyanide (10), present in certain foods (11), and formed during protein metabolism (10). In smokers, cigarette smoke is an important source of HCN (12).…”

Section: Introductionmentioning

confidence: 99%

Intake of Iodine and Perchlorate and Excretion in Human Milk

Dasgupta

Kirk

Dyke

et al. 2008

Environ. Sci. Technol.

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Perchlorate, thiocyanate, and iodine excretion in urine and milk of 13 breastfeeding women was investigated and the results were interpreted by a model of parallel/competitive transport of these species by the sodium iodide symporter. For each species i, we assumed physiological homeostasis, where i T,in equals the corresponding total excretion in urine and milk (i e,u + i e,m ). The fraction of the total excretion that appeared in milk f i,m was measured and ranged from 0.394-0.781, 0.018-0.144, and 0.086-0.464 for perchlorate, thiocyanate, and iodine, respectively. The corresponding median values were 0.541, 0.053, and 0.177, respectively. The selectivity factors of perchlorate over iodide transport, and thiocyanate over iodide transport, defined as f PC,m /f I,m , and f SCN,m /f I,m , respectively, were 3.14 ( 1.20 and 0.27 ( 0.26 while PC T,in , SCN T,in , and I T,in among individuals varied 4.9, 5.0, and 8.4×, respectively. These transport selectivities are an order of magnitude lower than those indicated by in vitro studies, suggesting that the impact of both these anions on inhibiting iodide transport in milk may have been overestimated in the extant literature. On the other hand, our results showed that 12 of 13 infants did not have an adequate intake of iodine as defined by the Institute of Medicine and 9 out of 13 infants were likely ingesting perchlorate at a level exceeding the reference dose suggested by the National Academy of Science panel.

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Enzymatic Conversion of Cyanide to Thiocyanate

Cited by 145 publications

References 0 publications

Presence of Rhodanese in the Cytosolic Fraction of the Fruit Bat (Eidolon helvum) Liver

Presence of Rhodanese in the Cytosolic Fraction of the Fruit Bat (Eidolon helvum) Liver

Tissue and intracellular distribution of rhodanese and mercaptopyruvate sulphurtransferase in ruminants and birds

Intake of Iodine and Perchlorate and Excretion in Human Milk

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