The DOI matches its Crossref record.
Some biochemical properties of Russell’s viper (Daboia russelli) venom from Eastern India: correlation with clinico-pathological manifestation in Russell’s viper bite
Abstract
In the present study, some biochemical properties and pathological effects of Daboia russelli venom from Burdwan district of West Bengal, eastern India are presented. The clinical features of Russell's viper envenomation observed in patients admitted to Burdwan Medical College & Hospital are also reported. In vitro, whole venom exerts strong trypsin inhibitory, phospholipase A2 and procoagulant activities in addition to moderate adenosine monophosphatase and adenosine triphosphatase activities. Lethality (LD50) of this venom sample is 0.7 mg kg (i.v.) of mice. Significant local tissue damaging effects including edema, hemorrhage and necrosis are observed in experimental animal models. An increase in the level of serum enzymes, such as aspartate transaminase, alkaline phosphatase, creatine phosphokinase, lactate dehydrogenase after D. russelli venom injection in albino rats is indicative of cell or tissue damage. High incidence of intravascular hemolysis in addition to hemostasis, haemoptysis and haematuria are observed as the most prominent features of RVV envenomation from this part of India. The present study reinforces the hypothesis that variation in the venom composition of RVV from eastern India with respect to venom samples of Russell's vipers from other parts of India is responsible for the differences in the clinical manifestation in patients from eastern India.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Such envenomation not only provokes an innate inflammatory response and pathology related to the biological activities of the venoms’ toxins [86–88], but also can induce allergic sensitization associated with the development of specific IgE antibodies [89–94].”
From Mast cells and IgE in defense against lethality of venoms: Possible “benefit” of allergy (2020) · cites this paper as [87]
Citations
Cites
No references could be resolved yet.
Research works printed but not linked: 38
- Aye-Kyaw, 1994, Purification, characterization and biological activities of phospholipase A from Russell’s viper (Vipera russelli) venom, Int. J. Biochem., 26, 79, 10.1016/0020-711X(94)90199-6 · DOI
- Bhat, 1989, Purification and characterization of myotoxic phospholipase A2 from Indian cobra (Naja naja naja) venom, Toxicon, 29, 861, 10.1016/0041-0101(89)90098-6 · DOI
- Bjarnason, 1988, Hemorrhagic toxins from snake venom, J. Toxicol. Toxin Rev., 7, 121, 10.3109/15569548809059729 · DOI
- Campbell, 1962, Assay of 5′-nucleotidase activity, vol. 1, 918
- Chakraborty, 1991, Lethal and hemorrhagic activity of Russell’s viper venom-neutralization by polyvalent, monovalent and toxoid antiserum, Ind. J. Exp. Biol., 29, 456
- Chakraborty, 1993, Purification and partial characterization of hemorrhagin (VRH-I) from Vipera russelli venom, Toxicon, 31, 1601, 10.1016/0041-0101(93)90344-I · DOI
- Dubois, 1956, Colorimetric method of determination of sugars and related substances, Analyt. Chem., 28, 350, 10.1021/ac60111a017 · DOI · Paper page
- Furukawa, 1976, Purification and characterization of a coagulant protein from the venom of Russell’s viper, Biochem. Biophys. Acta, 453, 48
- Gene, 1985, Neutralization of hyaluronidase and indirect hemolytic activities of Costa Rican snake venom by a polyvalent antivenom, Toxicon, 23, 1015, 10.1016/0041-0101(85)90397-6 · DOI
- Gene, 1989, Comparative study on coagulant, defibrinating, fibrinolytic activities of Costa Rican crotaline snake venoms and their neutralization by a polyvalent antivenom, Toxicon, 27, 841, 10.1016/0041-0101(89)90096-2 · DOI
- Hati, 1984, Snakebite in West Bengal of India, The Snake, 16, 129
- Hati, 1990, Active immunization of rabbits with gamma irradiated Russell’s viper venom toxoid, Toxicon, 28, 895, 10.1016/0041-0101(90)90019-4 · DOI
- Huang, 1984, Isolation and pharmacological properties of phospholipase A2 from Vipera russelli (Russell’s viper) snake venom, Toxicon, 22, 207, 10.1016/0041-0101(84)90021-7 · DOI
- Jayanthi, 1988, Geographical variation in India in the composition and lethal potency of Russell’s viper (Vipera russelli) venom, Toxicon, 26, 257, 10.1016/0041-0101(88)90216-4 · DOI
- Jeyarajah, 1984, Russell’s viper bite in Sir Lanka: A study of 22 cases, Am. J. Trop. Med. Hyg., 33, 506, 10.4269/ajtmh.1984.33.506 · DOI
- Kasturi, 1989, Purification and characterization of a major phospholipase A2 from Russell’s viper (Vipera russelli) venom, Toxicon, 27, 229, 10.1016/0041-0101(89)90136-0 · DOI
- Kini, 1982, Studies on snake venom enzymes. Part II—Partial characterization of ATPase from Russell’s viper (Vipera russelli) venom and their interaction with potassium gymnemate, Ind. J. Biochem. Biophys., 19, 342
- Larsen, 1968, The toxic proteins of cobra venom, Biochem-Pharmacol., 17, 503, 10.1016/0006-2952(68)90265-7 · DOI
- Lowry, 1951, Protein measurement with folin-phenol reagents, J. Biol. Chem., 193, 265, 10.1016/S0021-9258(19)52451-6 · DOI
- Maity, 1992, Study on the brain lipids of albino rats, The Snake, 24, 63
- Maung-Maung-Thwin, 1995, A major lethal factor of the venom of Burmese Russell’s viper (Daboia russelli siamensis): isolation, N-terminal sequencing and biological activities of daboiatoxin, Toxicon, 33, 63, 10.1016/0041-0101(94)00133-S · DOI
- Mittal, 1986, Renal lesions following viper bites—A study of 14 years, Ind. J. Med. Res., 83, 642
- Mukherjee, 1997, Lysosomal membrane stabilization by α-tocopherol against the damaging action of Vipera russelli venom phospholipase A2, Cell. Molec. Life Sci., 53, 152, 10.1007/PL00000586 · DOI
- Mukherjee, 1998, Effect of oral supplementation of vitamin E on the hemolysis and erythrocyte phospholipid splitting action of cobra and viper venoms, Toxicon, 36, 657, 10.1016/S0041-0101(97)00055-X · DOI
- Mukherjee, 1998, Composition of Naja naja venom samples from three districts of West Bengal, eastern India, Comp. Biochem. Physiol., 119, 621, 10.1016/S1095-6433(97)00475-3 · DOI
- Ouyang, 1976, Fibrinogenolytic enzymes of Trimeresurus mucrosquamatus venom, Biochim. Biophys. Acta, 420, 298, 10.1016/0005-2795(76)90321-4 · DOI
- Phillips, 1988, Paralysis, Rhabdomyolysis and hemolysis caused by bites of Russell’s viper (Vipera russelli pulchella) in Sri Lanka: failure of Indian (Haffkine) antivenom, Q. J. Med., 68, 691
- Sahu, 1989, Effects of envenomation on enzymes of brain of albino rats, Ind. J. Exp. Biol., 27, 831
- Sahu, 1991, Prospective study of some enyzmes in different parts of the rat’s brain following envenomation, The Snake, 23, 65
- Sharp, 1989, A basic phospholipase A from the venom of the Australian king brown snake (Pseudechis australis) showing diverse activities against membranes, Comp. Biochem. and Physiol., 92B, 501, 10.1016/0305-0491(89)90123-5 · DOI
- Soto, 1988, Proteolytic, hemorrhagic and hemolytic activities of snake venoms, Toxicon, 26, 875, 10.1016/0041-0101(88)90328-5 · DOI
- Than-Than, 1988, Haemostatic disturbances in patients bitten by Russell’s viper (Vipera russelli siamensis) in Burma, Br. J. Hematol., 69, 513, 10.1111/j.1365-2141.1988.tb02408.x · DOI
- Theakston, 1983, Development of simple standard assay procedures for the characterization of snake venoms, Bull. Wld. Hlth. Orag., 61, 949
- Tsai, 1996, Two types of Russell’s viper revealed by variation in phospholipase A2 from the venom of the subspecies, Toxicon, 34, 99, 10.1016/0041-0101(95)00114-X · DOI
- Tun-Pe, 1987, Acute and chronic pituitary failure resembling Sheehan’s syndrome following bites from Russell’s viper in Burma, Lancet, ii, 763, 10.1016/S0140-6736(87)92500-1 · DOI
- Vishwanath, 1988, Purification and partial biochemical characterization of an edema-inducing phospholipase A2 from Vipera russelli snake venom, Toxicon, 26, 713, 10.1016/0041-0101(88)90278-4 · DOI
- Warrell, 1989, Snake venom in science and clinical medicine. 1. Russell’s viper: biology, venom and treatment of bites, Trans. Roy. Soc. Trop. Med. Hyg., 83, 732, 10.1016/0035-9203(89)90311-8 · DOI
- Williams, 1962, The fractionation of Russell’s viper (Vipera russelli) venom with special reference to coagulant protein, Biochem. J., 84, 52, 10.1042/bj0840052 · DOI
Cited by
Sorted by citations
Mast cells and IgE in defense against venoms: Possible “good side” of allergy?
Galli, S. J., Starkl, P., Marichal, T., & Tsai, M. (2016) · Allergology International · doi:10.1016/j.alit.2015.09.002 · Cited by 73
Mast cells and IgE in defense against lethality of venoms: Possible “benefit” of allergy
Galli, S. J., Metz, M., Starkl, P., Marichal, T., & Tsai, M. (2020) · Allergo Journal International · doi:10.1007/s40629-020-00118-6 · Cited by 57
Metadata
- Authors
- Mukherjee, A. K., Ghosal, S. K., & Maity, C. R.
- Venue
- Toxicon
- Publisher
- Elsevier BV
- Published
- 2000-02
- Volume
- 38
- Issue
- 2
- Pages
- 163-175
- ISSN
- 0041-0101
- Cited by
- 82
- References
- 0
- Language
- en
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Some biochemical properties of Russell’s viper (Daboia russelli) venom from Eastern India: correlation with clinico-pathological manifestation in Russell’s viper bite. https://app.cochat.ai/papers/10.1016/s0041-0101(99)00125-7
- The paper
- Mukherjee, A. K., Ghosal, S. K., & Maity, C. R. (2000). Some biochemical properties of Russell’s viper (Daboia russelli) venom from Eastern India: correlation with clinico-pathological manifestation in Russell’s viper bite. Toxicon. https://doi.org/10.1016/s0041-0101(99)00125-7