Purification and Partial Characterisation of the Lectin from the Marine Red Alga Enantiocladia duperreyi (C. Agardh) Falkenberg

Benevídes, Norma Maria Barros; Araújo, Márjory Lima Holanda; Melo, Fabio Rabelo; Freitas, Ana Lúcia Ponte; Sampaio, Alexandre Holanda

doi:10.1515/botm.1998.41.1-6.521

Cited by 35 publications

(48 citation statements)

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“…However, the lectins from the red algae Ptilota serrata (Rogers et al 1990), Ptilota filicina (Sampaio, 1998b), Enantiocladia duperreyi (Benevides et al 1998a) and from the green algae Ulva laetevirens Areschoug (Sampaio et al 1996) and Ulva lactuca ) exhibited dependence of metals such as Ca 2+ , Mn 2+ and Mg 2+ , as is the case with most plant lectins. In accordance with Rogers & Hori (1993) lectins from the red algae do not require divalent cations for their biological activity.…”

Section: Resultsmentioning

confidence: 99%

“…The utilisation of affinity chromatography is also an important tool in the process of purification of algae lectins. Many lectins from these vegetables were isolated by this technique, such Ptilota filicina J. Agardh (Sampaio et al 1998b), Enantiocladia duperreyi (Benevides et al 1998a) and Caulerpa cupressoides (Benevides et al 2001). Most of the lectins isolated from marine red algae have low molecular weight (Rogers & Hori 1993).…”

Section: Discussionmentioning

confidence: 99%

“…The blood specificity from the Pterocladiella capillacea lectin was determined by use of erythrocytes from different animals (rabbit, chicken, ox, goat) and humans from the ABO system, native and treated with the enzymes trypsin, bromelain, papain and subtilisin, according to Benevides et al (1998a).…”

Section: Methodsmentioning

confidence: 99%

“…The hemagglutinating activity was assayed in the fractions obtained during the purification process according to Benevides et al (1998a). In small glass tubes a series of 1:2 dilutions (0.1 mL) of the protein fractions was mixed with 0.1 mL of a 2% suspension of enzyme-treated erythrocytes.…”

Section: Methodsmentioning

confidence: 99%

“…Schmitz and Ptilota serrata Kützing (Rogers et al 1990), Solieria filiformis (Kützing) Gabrielson (Benevides et al 1996) and Enantiocladia duperreyi (C. Agardh) Falkenberg (Benevides et al 1998a). Algal lectins differ from higher plant lectins in a variety of properties.…”

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Purification and characterisation of a lectin from the red marine alga Pterocladiella capillacea (S.G. Gmel.) Santel. & Hommers.

Oliveira¹,

Nascimento²,

Lima³

et al. 2002

Rev. bras. Bot.

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-(Purification and characterisation of a lectin from the red marine alga Pterocladiella capillacea (S.G. Gmel.) Santel. & Hommers.). A lectin present in the marine red alga Pterocladiella capillacea was purified and characterised by extraction of soluble proteins (crude extract) in 20 mM Tris-HCl buffer, pH 7.5. Among the analysed erythrocytes (human blood group A, B and O and the animals ox, goat, chicken and rabbit) the lectin agglutinated specifically rabbit erythrocytes. The hemagglutinating activity assay showed that the lectin was not dependent on divalent cations and was shown to be inhibited by the glycoproteins avidin and mucin. The purification procedure was conduced by precipitation of the crude extract with 80% saturation ammonium sulfate (F0/80) followed by affinity chromatography on guar-gum column. The lectin of P. capillacea was purified 14.5 fold and had a recovery of 27.4% of the original total specific activity present in the crude extract. The absence of carbohydrate suggested that the lectin is not a glycoprotein. The molecular mass of P. capillacea lectin, determined by gel filtration, was 5.8 kDa. SDS-PAGE in the presence of β-mercaptoethanol gave one band, indicating that the native lectin is a monomeric protein. The activation energy of denaturation process (∆G') was calculated to be 106.87 kJ . mol -1 at 70 o C.RESUMO -(Purificação e caracterização de uma lectina da alga marinha vermelha Pterocladiella capillacea (S.G. Gmel.) Santel. & Hommers.). Uma lectina presente na alga marinha vermelha Pterocladiella capillacea foi purificada e caracterizada pela extração de proteínas solúveis (extrato bruto) em tampão Tris-HCl 20 mM, pH 7,5. Entre os eritrócitos testados (grupos sangüíneos humanos A, B e O e os animais boi, cabra, galinha e coelho) a lectina aglutinou especificamente eritrócitos de coelho. O ensaio de atividade hemaglutinante evidenciou que a lectina não era dependente de cátions divalentes e inibida pelas glicoproteínas avidina e mucina. O procedimento de purificação foi conduzido por precipitação protéica do extrato bruto com sulfato de amônio até 80% de saturação (F 0/80), seguido por cromatografia de afinidade em coluna de goma de Guar. A lectina de P. capillacea foi purificada 14,5 vezes e teve uma recuperação de 27,4% da atividade específica total original presente no extrato bruto. A ausência de carboidrato sugeriu que a lectina não é uma glicoproteína. A massa molecular da lectina de P. capillacea, determinada por filtração em gel, foi de 5,8 kDa. PAGE-SDS em presença de β-mercaptoetanol mostou uma única banda protéica, indicando que a lectina de P. capillacea é uma proteína monomérica. A energia de ativação do processo de desnaturação (∆G') foi calculada em 106,87 kJ . mol -1 a 70 o C.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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Purification and characterisation of a lectin from the red marine alga Pterocladiella capillacea (S.G. Gmel.) Santel. & Hommers.

Oliveira¹,

Nascimento²,

Lima³

et al. 2002

Rev. bras. Bot.

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Purification and characterization of a novel haemagglutinin from Chlorella pyrenoidosa

Chu

Huang

Ling

2006

J Ind Microbiol Biotechnol

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We previously identified a strong haemagglutination activity in the freshwater unicellular green alga, Chlorella pyrenoidosa. Here, we sought to purify and characterize the haemagglutinin associated with this activity. Ammonium sulfate precipitation, gel filtration on sephacryl S-200 and DEAE-Sepharose ion-exchange chromatography were used to purify the haemagglutinin, which was designated CPH (Chlorella pyrenoidosa haemagglutinin). The molecular weight of CPH was estimated as 58 kDa by SDS-PAGE and 60 kDa by gel filtration of the native protein, indicating that this haemagglutinin exists as a monomer. The haemagglutinin activity of CPH was inhibited by glycoproteins, especially yeast mannan, but not by monosaccharides or disaccharides, indicating that CPH is carbohydrate-specific. In addition to the composition of CPH shown to be rich in glycine and acidic amino acids, heamagglutinating activity of CPH was insensitive to variations in pH or the presence of divalent cations, and atomic force microscopy revealed that the protein is rod-shaped. These results indicate that the characteristics of CPH are consistent with its identification as a haemagglutinin, and suggest that CPH may be a viable candidate for applications in a variety of biomedical fields.

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Protein extract from red seaweed Gracilaria fisheri prevents acute hepatopancreatic necrosis disease (AHPND) infection in shrimp

et al. 2016

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Purification and Partial Characterisation of the Lectin from the Marine Red Alga Enantiocladia duperreyi (C. Agardh) Falkenberg

Cited by 35 publications

References 6 publications

Purification and characterisation of a lectin from the red marine alga Pterocladiella capillacea (S.G. Gmel.) Santel. & Hommers.

Purification and characterisation of a lectin from the red marine alga Pterocladiella capillacea (S.G. Gmel.) Santel. & Hommers.

Purification and characterization of a novel haemagglutinin from Chlorella pyrenoidosa

Protein extract from red seaweed Gracilaria fisheri prevents acute hepatopancreatic necrosis disease (AHPND) infection in shrimp

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