• Title/Summary/Keyword: Naja naja

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Preliminary Study on the Antisnake Venom Activity of Alcoholic Root Extract of Clerodendrum viscosum (Vent.) in Naja naja Venom

  • Lobo, Richard;Punitha, I.S.R.;Rajendran, K.;Shirwaikar, Arun;Shirwaikar, Annie
    • Natural Product Sciences
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    • v.12 no.3
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    • pp.153-156
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    • 2006
  • The antisnake venom activity of Clerodendrum viscosum Vent. (Fam. Verbenaceae), a plant traditionally used in India for the treatment of snake bite was evaluated by in vitro and in vivo methods. While in vitro studies were performed using human blood, in vivo studies were carried out using mice administered three different i.p doses of the extract, 5 min before the administration of Naja naja snake venom. The results of the in vitro studies showed that the extract probably interacts with but does not stabilize membrane protein. In the in vivo studies the extract showed significant antisnake venom activity, which may be attributed to its possible interference with the acetylcholine receptor sites. Hence the present investigation justifies the traditional use of Clerodendrum viscosum (C. viscosum) as antisnake venom.

Modification of Substrate Inhibition of Synaptosomal Acetylcholinesterase by Cardiotoxins

  • Ranaei-Siadat, Seyed-Omid;Riazi, Gholam-Hosein;Sadeghi, Mehdi;Chang, Long-Sen;Lin, Shinne-Ren;Eghtesadi-Araghi, Peyman;Hakimelahi, Gholam Hossein;Moosavi-Movahedi, Ali Akbar
    • BMB Reports
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    • v.37 no.3
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    • pp.330-338
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    • 2004
  • Different types of cardiotoxin (I-V and n) were isolated and purified from the venom of the Taiwan cobra (Naja naja atra). The effects of these cardiotoxins were studied on membrane-bound acetylcholinesterase, which was isolated from a sheep's brain cortex. The results showed that cardiotoxins I-III, V, and n activated the enzyme by modification of substrate inhibition, but cardiotoxin IV's reaction was different. The inhibition and activation of acetylcholinesterase were linked to the functions of the hydrophobicity index, presence of a cationic cluster, and the accessible arginine residue. Our results indicate that Cardiotoxins have neither a cationic cluster nor an arginine residue in their surface area of loop I; therefore, in contrast to fasciculin, cardiotoxins are attached by loop II to the peripheral site of the enzyme. As a result, fasciculin seems to stabilize nonfunctional conformation, but cardiotoxins seem to stabilize the functional conformation of the enzyme. Based on our experimental and theoretical findings, similar secondary and tertiary structures of cardiotoxins and fasciculin seem to have an opposite function once they interact with acetylcholinesterase.

A study of ribonuclease activity in venom of vietnam cobra

  • Nguyen, Thiet Van;Osipov, A.V.
    • Journal of Animal Science and Technology
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    • v.59 no.9
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    • pp.20.1-20.9
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    • 2017
  • Background: Ribonuclease (RNase) is one of the few toxic proteins that are present constantly in snake venoms of all types. However, to date this RNase is still poorly studied in comparison not only with other toxic proteins of snake venom, but also with the enzymes of RNase group. The objective of this paper was to investigate some properties of RNase from venom of Vietnam cobra Naja atra. Methods: Kinetic methods and gel filtration chromatography were used to investigate RNase from venom of Vietnam cobra. Results: RNase from venom of Vietnam cobra Naja atra has some characteristic properties. This RNase is a thermostable enzyme and has high conformational stability. This is the only acidic enzyme of the RNase A superfamily exhibiting a high catalytic activity in the pH range of 1-4, with $pH_{opt}=2.58{\pm}0.35$. Its activity is considerably reduced with increasing ionic strength of reaction mixture. Venom proteins are separated by gel filtration into four peaks with ribonucleolytic activity, which is abnormally distributed among the isoforms: only a small part of the RNase activity is present in fractions of proteins with molecular weights of 12-15 kDa and more than 30 kDa, but most of the enzyme activity is detected in fractions of polypeptides, having molecular weights of less than 9 kDa, that is unexpected. Conclusions: RNase from the venom of Vietnam cobra is a unique member of RNase A superfamily according to its acidic optimum pH ($pH_{opt}=2.58{\pm}0.35$) and extremely low molecular weights of its major isoforms (approximately 8.95 kDa for RNase III and 5.93 kDa for RNase IV).

Physico-chemical Characteristics of Black Raspberry Fruits (Bokbunja) and Wines in Korea (산지별 복분자와 시판 복분자주의 이화학적 특성 분석)

  • Lee, Seung-Joo
    • Korean Journal of Food Science and Technology
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    • v.45 no.4
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    • pp.451-459
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    • 2013
  • Korean black raspberry fruits (bokbunja) were collected from 11 different producing regions, and commercial black raspberry wines were obtained from 24 manufacturers. Samples were analyzed for soluble solids, titratable acidity, pH, reducing sugar content, hunter color values, intensity, hue, total phenolic content, and organic acids. The fruit samples showed similar pH levels (3.43-3.52), but significantly differed in total acidity levels (9.98-16.2 g/L). The predominant organic acids in the fruit samples were citric acids (1.39-5.63 mg/mL) and succinic acids (0.25-6.53 mg/mL). Among the samples, black raspberry fruits from Goksung and Nonsan showed the lowest levels of total phenolic content, and the lowest values in intensity. The fruits from Jeongeup and Sunchang showed higher levels of phenolic content, soluble solids, and intensity. Some wine samples, including BH, KO, SR, and SE, showed overall high levels of phenolic content, organic acids like citric and succinic acid, and color values such as $a^*$, $b^*$, and intensity. Other wine samples, including DW, SC, GJ, and NB, were high in acetic acid, color values like $L^*$, and hue.