Purification and characterization of a low molecular weight multifunctional cytotoxic phospholipase A2 from Russell's viper venom☆

Maity, Gargi; Mandal, Somnath; Chatterjee, Amitabha; Bhattacharyya, Debasish

doi:10.1016/j.jchromb.2006.08.038

Cited by 26 publications

(17 citation statements)

References 45 publications

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“…Recently, an anti-tumoral activity was described for BthA-I-PLA2, an acidic PLA2 isolated from Bothrops jararacussu venom (Roberto et al, 2004) and for RVV-7, a basic 7 kDa toxin from Russell's viper venom (Maity et al, 2007). These two proteins exert an indirect anti-tumor activity through their cytotoxicity.…”

Section: Introductionmentioning

confidence: 99%

MVL-PLA2, a phospholipase A2 from Macrovipera lebetina transmediterranea venom, inhibits tumor cells adhesion and migration

et al. 2009

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Section: Introductionmentioning

confidence: 99%

MVL-PLA2, a phospholipase A2 from Macrovipera lebetina transmediterranea venom, inhibits tumor cells adhesion and migration

et al. 2009

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“…The crude enzyme as well as partially purified enzyme was evaluated for protease activity and thrombolytic activity. Furthermore, partially purified enzyme was concentrated by ultrafiltration through centricon tubes (Maity et al, 2007;Guerrieri et al, 2000). In this purification purpose, 100 kDa MWCO and 30 kDa MWCO centricon tubes (Amicon®, Millipore) were used and proteins were concentrated by centrifugation at 5,000 g for 15 minutes (2.5×30 cm, Amersham Biosciences, Sweden).…”

Section: Purification Of Enzymementioning

confidence: 99%

Thrombolytic Activity of Alkaline Protease Purified from a Mutant Strain Bacillus licheniformis MZK05M9

Zaman¹,

Akhtar²,

Azam³

et al. 2018

Bangla Pharma J

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Investigations were performed to find out new microbial enzymes as thrombolytics having better efficacy and specificity. Mutant strain of Bacillus species, B. licheniformis MZK05M9 was cultured in modified urea-glucose media followed by purification using ammonium sulphate precipitation and ultrafiltration through centricon tube of specific MWCO value. The production method yielded 823.42 units/mg of the crude enzyme from mutant strain MZK05M9 and after purification 37695.64 units/mg. The molecular weight of the purified enzyme was estimated as 27.2 kDa and purification increased its specific activity to 16.5 fold with a recovery of 10%. The purified proteases were identified as serine proteases by irreversible inhibition of activity with phenylmethylsulfonyl fluoride (PMSF) and it exhibited 32.84% thrombolytic activity, by in vitro clot lysis assay. Stability studies showed that crude enzyme from mutant strain MZK05M9 remained stable up to a temperature of 45˚C and showed maximum stability at pH range 7.5 to 8.5. Our observation indicates that proteases produced by Bacillus licheniformis mutant have the potential to be developed as a viable thrombolytic agent.

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“…The precipitate obtained was dissolved in 50 mM Tris-HCl buffer (pH 7.0). 19,20 This partially purified enzyme was then concentrated by ultrafiltration passing through centricon tubes (Amicon®, Millipore) 21,22 of 100 kDa MWCO and 30 kDa MWCO.…”

Section: Microorganism and Culturementioning

confidence: 99%

Partial Purification of Alkaline Protease as Thrombolytic Agent from Mutant Strain Bacillus licheniformis EMS250-O-1

Zaman

Mamun

Khan

et al. 2017

Dhaka Univ. J. Pharm. Sci

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Thrombosis leads to myocardial infarction, stroke and other cardiovascular complications. Microbial thrombolytic agents such as urokinase, streptokinase etc. are used to treat complications related to thrombosis. To search for new microbial enzymes as thrombolytics having better efficacy and specificity, Bacillus licheniformis EMS-O-1 mutant strain was cultured in modified urea-molasses media followed by purification using ammonium sulphate precipitation and ultrafiltration through centricon tube of 100 MWCO value. The yield of crude enzyme was 11129.14 U/mg and after purification 40180.46 U/mg. Purification process increased the specific activity of purified enzyme to 12.28 fold with a recovery of 17.79%. The purified enzyme was a serine protease with molecular weight of 25.5 kDa as confirmed by irreversible inhibition of activity with phenylmethylsulfonyl fluoride (PMSF) followed by SDS-PAGE gel image and by LC-MS analyses. In vitro clot lysis assay of the purified enzyme exhibited 38.30% thrombolytic activity. The crude enzymes from the mutant strain EMS-O-1 were found to be stable up to 50 o C and showed maximum stability between pH range 7.5 to 8.5. These findings signify that proteases produced by B. licheniformis mutant have the potential to be developed as a viable thrombolytic agent.

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Purification and characterization of a low molecular weight multifunctional cytotoxic phospholipase A2 from Russell's viper venom☆

Cited by 26 publications

References 45 publications

MVL-PLA2, a phospholipase A2 from Macrovipera lebetina transmediterranea venom, inhibits tumor cells adhesion and migration

MVL-PLA2, a phospholipase A2 from Macrovipera lebetina transmediterranea venom, inhibits tumor cells adhesion and migration

Thrombolytic Activity of Alkaline Protease Purified from a Mutant Strain Bacillus licheniformis MZK05M9

Partial Purification of Alkaline Protease as Thrombolytic Agent from Mutant Strain Bacillus licheniformis EMS250-O-1

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