Biochemical and molecular modeling analysis of the ability of two p-aminobenzamidine-based sorbents to selectively purify serine proteases (fibrinogenases) from snake venoms

De-Simone, Salvatore Giovanni; Corrêa-Netto, Carlos; Antunes, Octávio Augusto Ceva; De-Alencastro, R.B.; Silva, F.P.

doi:10.1016/j.jchromb.2005.04.018

Cited by 36 publications

(17 citation statements)

References 44 publications

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“…Therefore, the searche for other fibrinolytic enzymes from various sources continues. Over the last decade, potent fibrinolytic enzymes have been discovered from a variety of sources, such as earthworms, 4,5) snake venom, 6,7) insects, 8) food-grade microorganisms, 9) marine creatures, 10) and fermented food products such as Japanese natto, 11) Korean chungkook-jang, 12) and Chinese douchi. 13) In recent years, mushroom have become an attractive source of various physiologically active compounds.…”

Section: Purification and Characterization Of A Fibrinolytic Proteasementioning

confidence: 99%

Purification and Characterization of a Fibrinolytic Protease from a Culture Supernatant ofFlammulina velutipesMycelia

Park¹,

Li²,

Kim³

et al. 2007

Bioscience, Biotechnology, and Biochemistry

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Section: Purification and Characterization Of A Fibrinolytic Proteasementioning

confidence: 99%

Purification and Characterization of a Fibrinolytic Protease from a Culture Supernatant ofFlammulina velutipesMycelia

Park¹,

Li²,

Kim³

et al. 2007

Bioscience, Biotechnology, and Biochemistry

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“…Over the last 10 years, several effective thrombolytic agents have been identified and characterized from microorganisms [4][5][6], earthworms [7], snake venoms [8,9], centipede venoms [10], insects [11], and leeches [12]. The agents are of interest as useful tools for understanding fibrinolytic mechanism and as potential therapeutic drugs.…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of a fibrinolytic enzyme of Bacillus subtilis DC33, isolated from Chinese traditional Douchi

Wang

Лі

et al. 2006

J IND MICROBIOL BIOTECHNOL

150

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Bacillus subtilis DC33 producing a novel fibrinolytic enzyme was isolated from Ba-bao Douchi, a traditional soybean-fermented food in China. The strong fibrin-specific enzyme subtilisin FS33 was purified to electrophoretic homogeneity using the combination of various chromatographic steps. The optimum temperature, pH value, and pI of subtilisin FS33 were 55°C, 8.0, and 8.7, respectively. The molecular weight was 30 kDa measured by SDS-PAGE under both reducing and non-reducing conditions. The enzyme showed a level of fibrinolytic activity that was about six times higher than that of subtilisin Carlsberg. The first 15 amino acid residues of N-terminal sequence of the enzyme were A-Q-S-V-P-Y-G-I-P-Q-I-K-A-P-A, which are different from that of other known fibrinolytic enzymes. The amidolytic activities of subtilisin FS33 were inhibited completely by 5 mM phenylmethanesulfonyl fluoride (PMSF) and 1 mM soybean trypsin inhibitor (SBTI), but 1,4-dithiothreitol (DTT), b-mercaptoethanol, and p-hydroxymercuribenzoate (PHMB) did not affect the enzyme activity; serine and tryptophan are thus essential in the active site of the enzyme. The highest affinity of subtilisin FS33 was towards N-Succ-Ala-Ala-Pro-PhepNA. Therefore, the enzyme was considered to be a subtilisin-like serine protease. The fibrinolytic enzyme had a high degrading activity for the Bb-chains and Aa-chain of fibrin(ogen), and also acted on thrombotic and fibrinolytic factors of blood, such as plasminogen, urokinase, thrombin, and kallikrein. So subtilisin FS33 was able to degrade fibrin clots in two ways, i.e., (a) by forming active plasmin from plasminogen and (b) by direct fibrinolysis.

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“…However, the sample capacity and inefficiency of gel-filtration chromatography step made the protocol time consuming and productivity low in production scale [7,9,12,14]. Another affinity chromatography protocol was also reported [15], but the recovery of activity was low.…”

Section: Introductionmentioning

confidence: 99%

Affinity purification of serine proteinase from Deinagkistrodon acutus venom

Xin¹,

Dong²,

Wang³

et al. 2007

Journal of Chromatography B

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Biochemical and molecular modeling analysis of the ability of two p-aminobenzamidine-based sorbents to selectively purify serine proteases (fibrinogenases) from snake venoms

Cited by 36 publications

References 44 publications

Purification and Characterization of a Fibrinolytic Protease from a Culture Supernatant ofFlammulina velutipesMycelia

Purification and Characterization of a Fibrinolytic Protease from a Culture Supernatant ofFlammulina velutipesMycelia

Purification and characterization of a fibrinolytic enzyme of Bacillus subtilis DC33, isolated from Chinese traditional Douchi

Affinity purification of serine proteinase from Deinagkistrodon acutus venom

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