Purification, Biochemical and Functional Characterization of Miliin, a New Thiol-Dependent Serine Protease Isolated from the Latex of Euphorbia milii

Moro, Laís; Murakami, Mitsuru; Cabral, Hamilton; Vidotto, Alessandra; Tajara, Eloíza H.; Arni, R.K.; Juliano, Luis; Bonilla-Rodriguez, Gustavo Orlando

doi:10.2174/092986608785133744

Cited by 17 publications

(14 citation statements)

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“…These results confirm data obtained by Duarte et al (2009), suggesting that this plant has one or more enzymes with rennet-like. Usually, plants with latex have several proteases, as is the case of Euphorbia dupifera, Euphorbia milli (Moro et al, 2008) and others.…”

Section: Discussionmentioning

confidence: 99%

New peptides obtained by hydrolysis of caseins from bovine milk by protease extracted from the latex Jacaratia corumbensis

Arruda

Silva

Egito

et al. 2012

LWT

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Section: Discussionmentioning

confidence: 99%

New peptides obtained by hydrolysis of caseins from bovine milk by protease extracted from the latex Jacaratia corumbensis

Arruda

Silva

Egito

et al. 2012

LWT

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“…Proteolytic activity observed in only one peak suggests the existence of only one protease in the latex of S. asper. Such a single protease is an uncommon feature, as plant latex consists of several proteases, e.g., Euphorbia dupifera (Lynn & Clevette-Radford, 1988), Euphorbia milli (Moro et al, 2008;Yadav et al, 2006) and others. To the best of our knowledge, this is the first report of identification and purification of a serine protease from the genus Streblus of the Moraceae family.…”

Section: Purification Of the Enzymementioning

confidence: 99%

Purification and biochemical characterisation of a novel protease streblin

2011

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“…However, serine proteases are found in the latex of Euphorbiaceae. This type of enzyme was obtained, for example, from the latex of Euphorbia supina (Arima et al, 2000) and Euphorbia milii, with potential applications in food industry (Yadav, Pande, Jagannadham, 2006;Moro et al, 2008;Fonseca et al, 2010). Also from Euphorbia hirta, a serine protease, with fibrinolytic activity and potential industrial and therapeutic applications, was purified (Patel, Kawale, Sharma, 2012).…”

Section: Resultsmentioning

confidence: 99%

Proteinase activity in latex of three plants of the family Euphorbiaceae

Sobottka

Tonial

Sytwala

et al. 2014

Braz. J. Pharm. Sci.

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In the family of Euphorbiaceae, the genera Euphorbia and Sapium are known to contain essentially latex-bearing species. In the present study, the latex of Euphorbia selloi (Klotzsch & Garcke) Boiss., Euphorbia papillosa A.St.-Hil., and Sapium glandulosum (L.) Morong, plants native from Brazil, were examined concerning proteolytic activity. All studied species have proteins with significant proteolytic activity and E. papillosa has the greatest specific activity. Aiming to verify the type of protease present, an assay with different inhibitors was performed. In the three tested plants, the proteolytic activity was significantly inhibited by a serine protease inhibitor 4-(2-aminoethyl)-benzenesulfonyl fluoride hydrochloride (AEBSF). Using techniques of electrophoresis with polyacrylamide gels (SDS-PAGE), the subunits of proteins were separated according to their molecular masses, and the protein activity was visually detected by zymography.Uniterms: Euphorbiaceae/species/phytochemistry. Euphorbia papillosa/phytochemistry. Euphorbia selloi/ phytochemistry. Sapium glandulosum/phytochemistry. Euphorbia papillosa/proteinase activity. Euphorbia selloi/proteinase activity. Sapium glandulosum/proteinase activity. Endopeptidase. Gel electrophoresis.Dentro da família Euphorbiaceae, os gêneros Euphorbia e Sapium são conhecidos por incluírem basicamente espécies produtoras de látex. No presente estudo, o látex das plantas Euphorbia selloi (Klotzsch & Garcke) Boiss., Euphorbia papillosa A.St.-Hil. e Sapium glandulosum (L.) Morong, espécies nativas do Brasil, foi analisado em relação à atividade proteolítica. Todas as amostras analisadas possuem proteínas com significativa atividade, sendo que o látex da espécie E. papillosa apresenta a maior atividade específica. Com o objetivo de analisar quais os tipos de proteases responsáveis pela atividade proteolítica, realizaram-se ensaios com diferentes inibidores. Nas três plantas testadas a atividade foi inibida significativamente pelo cloridrato de 4-(fluoreto de 2-aminoetilbenzenossulfonil) (AEBSF), um inibidor de serino-proteases. Utilizando técnicas de eletroforese em gel de poliacrilamida (SDS-PAGE), as subunidades das proteínas foram separadas de acordo com sua massa molecular e, através da zimografia, a atividade proteolítica pode ser detectada visualmente. Unitermos

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Purification, Biochemical and Functional Characterization of Miliin, a New Thiol-Dependent Serine Protease Isolated from the Latex of Euphorbia milii

Cited by 17 publications

References 0 publications

New peptides obtained by hydrolysis of caseins from bovine milk by protease extracted from the latex Jacaratia corumbensis

New peptides obtained by hydrolysis of caseins from bovine milk by protease extracted from the latex Jacaratia corumbensis

Purification and biochemical characterisation of a novel protease streblin

Proteinase activity in latex of three plants of the family Euphorbiaceae

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