scholarly journals Identification and hemolytic activity of jellyfish (Rhopilema sp., Scyphozoa: Rhizostomeae) venom from the Persian Gulf and Oman Sea

2019 ◽  
Vol 20 (4) ◽  
pp. 1228-1232
Author(s):  
HOSSEIN JAFARI ◽  
HOSSEIN HONARI ◽  
JAMIL ZARGAN ◽  
SAEID TAMADONI JAHROMI
Keyword(s):  
Hemolytic Activity ◽  
Persian Gulf ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Biologically Active ◽  
Major Protein ◽  
Crude Venom ◽  
Oman Sea ◽  
Protein Components ◽  
The Persian Gulf

Abstract. Jafari H, Honari H, Zargan J, Jahromi ST. 2019. Identification and hemolytic activity of jellyfish (Rhopilema sp., Scyphozoa: Rhizostomeae) venom from the Persian Gulf and Oman Sea. Biodiversitas 20: 1228-1232. The present study investigated the hemolytic capacity of the crude venom extracted from isolated nematocysts of Rhopilema sp. Scyphozoa: Rhizostomeae. Nematocyst was used at various concentrations to evaluate the hemolytic activity by using the nematocysts of human, mice, and sheep. Mean concentration-dependent hemolysis could be observed from 200 µg/mL of protein equivalents or higher with variable potencies in different species. The crude venom was analyzed using sodium dodecyl sulfate-polyacrylamide gel electrophoresis SDS-PAGE. Molecular weight with 3 clear bands including 45, 65 and 95 kDa appeared to be the major protein components of the venom. The results of our experiments indicated that venom of Rhopilema sp. induces hemolysis in the studied species and determined that the increase in the amount of toxin has a positive correlation with the increase of cell lysis. This study showed that the venom of Rhopilema sp. may have many biologically active principles, which need further studies in the future.

Membranes of chromaffin granules. Isolation and partial characterization of two proteins

1971 ◽  
Vol 122 (3) ◽  
pp. 298.1-304 ◽  
Author(s):  
Heide Hörtnagl ◽  
H. Winkler ◽  
J. A. L. Schöpf ◽  
W. Hohenwallner
Keyword(s):  
Membrane Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein A ◽  
Sodium Dodecyl ◽  
Major Protein ◽  
Chromaffin Granules ◽  
Protein Components ◽  
Acid Gel ◽  
Total Membrane

Membranes of chromaffin granules were isolated from the adrenal glands of four different species. The solubilized membrane proteins could be resolved into several bands by polyacrylamide-gel electrophoresis (alkaline and acid gel systems). Two major protein components appeared to be common to the chromaffin granule membranes of ox, horse, pig and man. The various membrane proteins of bovine chromaffin granules were separated by filtration on Sephadex G-200 in the presence of sodium dodecyl sulphate. Two major membrane proteins (A and B) were obtained in purified form. Treatment of protein A with 2-mercaptoethanol before electrophoresis resulted in two more rapidly migrating subunits, whereas protein B was unaffected by mercaptoethanol treatment. The amino acid compositions of the two purified proteins were determined. They are very similar to that of the total membrane proteins but significantly different from that of the chromogranins, the soluble proteins of chromaffin granules.

Studies on the Stellaria longipes complex (Caryophyllaceae). VII. The seed proteins

1986 ◽  
Vol 64 (7) ◽  
pp. 1327-1330 ◽  
Author(s):  
David J. Gifford ◽  
C. C. Chinnappa
Keyword(s):  
Species Complex ◽  
Polyacrylamide Gel Electrophoresis ◽  
General Pattern ◽  
Sodium Dodecyl ◽  
Seed Proteins ◽  
Distinct Species ◽  
Major Protein ◽  
Stellaria Longipes ◽  
Cytogenetic Studies ◽  
Protein Components

Seed proteins of Stellaria longipes s.l. 2n = 52, 78, and 104, have been characterized using sodium dodecyl sulphate – polyacrylamide gel electrophoresis. The same general pattern as regards the number of major protein components resolved was observed in all the genotypes and cytotypes studied. These included all the morphotypes that were described as distinct species. The present data do not contradict the conclusions drawn from cytogenetic studies that all the morphological types are closely related and are part of a polyploid species complex.

A metalloproteinase extracellularly released byCrithidia deanei

2003 ◽  
Vol 49 (10) ◽  
pp. 625-632 ◽  
Author(s):  
Claudia Masini d'Avila-Levy ◽  
Rodrigo F Souza ◽  
Rosana C Gomes ◽  
Alane B Vermelho ◽  
Marta H Branquinha
Keyword(s):  
Molecular Mass ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Residual Activity ◽  
Major Protein ◽  
Motile Cells ◽  
Sds Page ◽  
Triton X

Actively motile cells from a cured strain of Crithidia deanei released proteins in phosphate buffer (pH 7.4). The molecular mass of the released polypeptides, which included some proteinases, ranged from 19 to 116 kDa. One of the major protein bands was purified to homogeneity by a combination of anion-exchange and gel filtration chromatographs. The apparent molecular mass of this protein was estimated to be 62 kDa by sodium dodecyl sulfate – polyacrylamide gel electrophoresis (SDS–PAGE). The incorporation of gelatin into SDS–PAGE showed that the purified protein presented proteolytic activity in a position corresponding to a molecular mass of 60 kDa. The enzyme was optimally active at 37 °C and pH 6.0 and showed 25% of residual activity at 28 °C for 30 min. The proteinase was inhibited by 1,10-phenanthroline and EDTA, showing that it belonged to the metalloproteinase class. A polyclonal antibody to the leishmanial gp63 reacted strongly with the released C. deanei protease. After Triton X-114 extraction, an enzyme similar to the purified metalloproteinase was detected in aqueous and detergent-rich phases. The detection of an extracellular metalloproteinase produced by C. deanei and some other Crithidia species suggests a potential role of this released enzyme in substrate degradation that may be relevant to the survival of trypanosomatids in the host.Key words: endosymbiont, trypanosomatid, extracellular, proteinase.

scholarly journals Isolation, partial purification and characterization of phospholipase A2 from Naja Katiensis venom

2021 ◽  
Vol 13 (2) ◽  
pp. 107-112
Author(s):  
C.F. Okechukwu ◽  
P.L. Shamsudeen ◽  
R.K. Bala ◽  
B.G. Kurfi ◽  
A.M. Abdulazeez
Keyword(s):  
Ion Exchange ◽  
Phospholipase A2 ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Partial Purification ◽  
Crude Venom

The most effective and acceptable therapy for snakebite victims is the immediate administration of antivenin which is limited by problems of hypersensitivity reactions in some individuals and its inability to resolve the local effects of the venom. The aim of this study was to isolate, partially purify and characterize phospholipase A2 from Naja Katiensis venom. Phospholipase A2 was partially purified via a two-step process: gel filtration on Sephadex G-75 and ion exchange chromatography using CM Sephadex, and subjected to SDS-PAGE analysis. From the results, the specific activity of the partially purified PLA2 decreased from 0.67μmol/min/mg in crude venom to 0.29μmol/min/mg after ion exchange chromatography with a yield of 5% and purification fold of 0.43. The optimum temperature of the purified PLA2 was found to be 35ºC and optimum p.H of 7. velocity studies for the determination of kinetic constants using L-a-lecithin as substrate revealed a Km  of 1.47mg/ml and Vmax  of 3.32μ moles/min/mg. The sodium dodecyl sulphate polyacrylamide gel electrophoresis of the purified PLA2 showed a distinct band with molecular weight estimated to be 14KDa. In conclusion, the present study shows that phospholipase A2 was isolated, purified and characterized. This may serve as a promising candidate for future development of a novel anti-venin drug.

scholarly journals The structure of the Persian Gulf outflow subjected to density variations

2008 ◽  
Vol 5 (2) ◽  
pp. 135-161 ◽  
Author(s):  
A. A. Bidokhti ◽  
M. Ezam
Keyword(s):  
Mass Transport ◽  
Persian Gulf ◽  
Anthropogenic Factors ◽  
Oman Sea ◽  
The Earth ◽  
Salinity Increase ◽  
Persian Gulf Water ◽  
Oceanographic Data ◽  
The Persian Gulf ◽  
Simple Dynamical Model

Abstract. Oceanographic data and a dynamic model are used to consider the structure of Persian Gulf outflow. This outflow influences the physical properties of Oman seawater which appear in the CTD profiles of the Oman Sea. The observations show that thickness of the outflow, which is banked against the Oman coasts due to the earth rotation, is about 200 m with tongues extending east and north that may be due to the internal waves. A simple dynamical model of the outflow based on potential vorticity conservation is used to find the horizontal extension of the outflow from the coast. Typical mass transport estimate by the outflow is about 0.4 Sv, which is larger than those reported by others. This may be due to the fact the model is inviscid but the outflow is influenced by the bottom friction. Variability of the outflow structure may reflect the changing ecosystem of the Persian Gulf. Any change of the outflow source, the Persian Gulf Water (PGW), say salinity increase due to excessive evaporation (climate factor) or desalination (anthropogenic factors) of the PGW may change the outflow structure and the product waters in the Oman Sea. Hence, one can test different scenarios of changing the outflow source, the Persian Gulf Water (PGW), say by salinity increase due to excessive evaporation or desalination (ecosystem factors) of the PGW to estimate changes in the outflow structure and the product waters in the Oman Sea. The results of the model show that these can increase the outflow width and mass transport substantially.

scholarly journals Venomics and Cellular Toxicity of Thai Pit Vipers (Trimeresurus macrops and T. hageni)

Toxins ◽  
2020 ◽  
Vol 12 (1) ◽  
pp. 54 ◽  
Author(s):  
Supeecha Kumkate ◽  
Lawan Chanhome ◽  
Tipparat Thiangtrongjit ◽  
Jureeporn Noiphrom ◽  
Panithi Laoungboa ◽  
...  
Keyword(s):  
Snake Venom ◽  
Protein Composition ◽  
Treatment Method ◽  
Cross Reactivity ◽  
Major Protein ◽  
Dependent Manner ◽  
Crude Venom ◽  
Monocytic Cells ◽  
Protein Components ◽  
Species Specific

The two venomous pit vipers, Trimeresurus macrops and T. hageni, are distributed throughout Thailand, although their abundance varies among different areas. No species-specific antivenom is available for their bite victims, and the only recorded treatment method is a horse antivenom raised against T. albolabris crude venom. To facilitate assessment of the cross-reactivity of heterologous antivenoms, protein profiles of T. macrops and T. hageni venoms were explored using mass-spectrometry-based proteomics. The results show that 185 and 216 proteins were identified from T. macrops and T. hageni venoms, respectively. Two major protein components in T. macrops and T. hageni venoms were snake venom serine protease and metalloproteinase. The toxicity of the venoms on human monocytes and skin fibroblasts was analyzed, and both showed a greater cytotoxic effect on fibroblasts than monocytic cells, with toxicity occurring in a dose-dependent rather than a time-dependent manner. Exploring the protein composition of snake venom leads to a better understanding of the envenoming of prey. Moreover, knowledge of pit viper venomics facilitates the selection of the optimum heterologous antivenoms for treating bite victims.

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