| Name | hemoglobin (protein family or complex) |
|---|---|
| Synonyms | Hemoglobin; Hemoglobins |
| Name | carbon disulfide |
|---|---|
| CAS | carbon disulfide |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 9498226 | Valentine WM, Amarnath V, Amarnath K, Erve JC, Graham DG, Morgan DL, Sills RC: Covalent modification of hemoglobin by carbon disulfide: III. Neurotoxicology. 1998 Feb;19(1):99-107. |
83(1,1,1,3) | Details |
| 2845535 | Masuda Y, Yasoshima M, Shibata K: Effects of carbon disulfide, diethyldithiocarbamate, and disulfiram on drug metabolism in the perfused rat liver. Res Commun Chem Pathol Pharmacol. 1988 Jul;61(1):65-82. The effects of carbon disulfide (CS2), diethyldithiocarbamate (DTC) and disulfiram (DS) on hepatic drug metabolism were studied in a noncirculating and hemoglobin-free rat liver perfusion system using p-nitroanisole (p-NA) as a substrate. |
81(1,1,1,1) | Details |
| 5120383 | Blevins DI, Miller CC, Kleckner MD: Effects of a piperazine-carbon disulfide-phenothiazine preparation on hemoglobin and packed cell values of horses. J Am Vet Med Assoc. 1971 Nov;159(10):1260-2. |
6(0,0,1,1) | Details |
| 7727395 | Ensign SA: Reactivity of dehydrogenase from Rhodospirillum rubrum with carbonyl sulfide, and carbon disulfide. Biochemistry. 1995 Apr 25;34(16):5372-8. CO was a potent inhibitor of CO2 reduction at dissolved concentrations as low as 1 microM, but this inhibition could be prevented by quantitatively trapping CO as it was formed by including reduced hemoglobin in the assays. |
2(0,0,0,2) | Details |
| 3787622 | Lam CW, DiStefano V: Characterization of carbon disulfide binding in blood and to other biological substances. Toxicol Appl Pharmacol. 1986 Nov;86(2):235-42. Incubation of fractionated human RBC lysates with CS2 showed that CS2 binding in these fractions was proportional to the hemoglobin concentration. |
2(0,0,0,2) | Details |
| 8722110 | Costa LG: Biomarker research in neurotoxicology: the role of mechanistic studies to bridge the gap between the laboratory and epidemiological investigations. Environ Health Perspect. 1996 Mar;104 Suppl 1:55-67. This review discusses several aspects of biomarker research as it relates to compounds and focuses on selected agents (organophosphorus insecticides, styrene, n-hexane, carbon disulfide, acrylamide), which have been the subject of a number of investigations in animals and humans. While traditional biomonitoring approaches and novel techniques (e.g., hemoglobin adducts) provide several measurements for monitoring exposure to chemicals, potential markers of genetic susceptibility have been seldom investigated in a neurotoxicology context. |
1(0,0,0,1) | Details |
| 9473537 | Johnson DJ, Graham DG, Amarnath V, Amarnath K, Valentine WM: Release of carbon disulfide is a contributing mechanism in the axonopathy produced by N,N-diethyldithiocarbamate. Toxicol Appl Pharmacol. 1998 Feb;148(2):288-96. At the end of each treatment period, erythrocyte spectrin, hemoglobin, and spinal cord neurofilament preparations were isolated and examined for cross-linking using polyacrylamide gel electrophoresis, reverse phase HPLC, and Western blot techniques, respectively. |
1(0,0,0,1) | Details |
| 11005259 | Tonkin EG, Erve JC, Valentine WM: Disulfiram produces a non-carbon disulfide-dependent schwannopathy in the rat. J Neuropathol Exp Neurol. 2000 Sep;59(9):786-97. Male Sprague-Dawley rats were administered 1% w/w disulfiram in their feed for 2, 4, 5, or 7 wk, and erythrocyte spectrin, hemoglobin, and neurofilament preparations were isolated and the extent of cross-linking assessed by SDS-PAGE, RP-HPLC, and Western blotting, respectively. |
1(0,0,0,1) | Details |
| 9778308 | Erve JC, Amarnath V, Sills RC, Morgan DL, Valentine WM: Characterization of a - thiourea cross-link on rat globin produced by carbon disulfide or N,N-diethyldithiocarbamate in vivo. Chem Res Toxicol. 1998 Oct;11(10):1128-36. In vitro incubation of human hemoglobin with either CS2 or N, N-diethyldithiocarbamate also resulted in the formation of CS2-generated - thiourea. |
1(0,0,0,1) | Details |
| 15218747 | Muzi G, Locati EH, Murgia N, Ambrosio G, Abbritti G: [Evaluation of the effects of occupational noxae on the cardiovascular system]. Med Lav. 2004 Mar-Apr;95(2):145-57. In occupational and environmental studies ultrasound measurement of intima-medial carotid thickness and brachial artery reactivity have been used to determine the effects of exposure to carbon disulfide and passive smoking. Some blood chemistry parameters that may be modified by occupational exposure or by particular conditions arising from work organization are triglycerides, apolipoproteins A and B, platelets, fibrinogen, factor VIIc, fibrinolysis products, plasminogen tissue activating factor, complement and glycated hemoglobin. |
1(0,0,0,1) | Details |
| 3700964 | Lam CW, DiStefano V, Morken DA: The role of the red blood cell in the transport of carbon disulfide. . J Appl Toxicol. 1986 Apr;6(2):81-6. It was found that 98% of the free CS2 in red blood cell lysates was associated with hemoglobin. |
1(0,0,0,1) | Details |
| 2250405 | Yoshida A, Morozumi K, Oikawa T, Suganuma T, Aoki J, Sugito K, Koyama K, Fujinami T, Shigematsu H: Nodular glomerulosclerosis in a patient showing impaired glucose tolerance. Nippon Jinzo Gakkai Shi. 1990 Aug;32(8):877-84. In an extensive examination for DM, the results of funduscopy, daily profile of serum and hemoglobin Alc were entirely within normal limits. Although hypocellular nodular lesions by light microscopy are characteristic of diabetic nephropathy, renal amyloidosis, carbon disulfide intoxication, multiple myeloma and light chain disease, we concluded that the present lesions had resulted from diabetic nephropathy based on the family history, patient history, impaired glucose tolerance, immunofluorescent findings and electron microscopic observations. |
1(0,0,0,1) | Details |
| 7727396 | Seefeldt LC, Rasche ME, Ensign SA: Carbonyl sulfide and as new substrates, and carbon disulfide as a new inhibitor, of nitrogenase. Biochemistry. 1995 Apr 25;34(16):5382-9. In this assay, the change in the visible absorption spectrum of reduced hemoglobin upon binding CO provided a sensitive way to quantify CO formation and to remove CO, which is a potent inhibitor of nitrogenase, from solution. |
1(0,0,0,1) | Details |