NDLI: Purification and Biological Activities of Abelmoschus esculentus Seed Lectin

Content Provider	Springer Nature Link
Author	Sousa Ferreira Soares, Geórgia Assreuy, Ana Maria Sampaio Almeida Gadelha, Carlos Alberto Morais Gomes, Vinicius Delatorre, Plinio Conceição Simões, Rafael Cavada, Benildo Sousa Leite, Joana Filomena Naga, Celso Shiniti Pinto, Nilson Vieira Luna Freire Pessoa, Hilzeth Santi Gadelha, Tatiane
Copyright Year	2012
Abstract	The Abelmoschus esculentus (Malvaceae) plant originated in Africa and has spread across a number of tropic countries, including northeastern Brazil. The plant has been used to treat various disorders, such as cancer, microbial infections, hypoglycemia, constipation, urine retention and inflammation. The lectin of A. esculentus (AEL) was isolated by precipitation with ammonium sulfate at a saturation level of 30/60 and purified by ion exchange chromatography (Sephacel-DEAE). The electrophoresis (SDS-PAGE) profile of the AEL showed two protein bands of apparent molecular mass of approximately 15.0 and 21.0 kDa. The homogenity of the protein was confirmed by electrospray mass spectrometry (ESI-MS), which revealed the presence of a 10.29-kDa monomer and a 20.58-kDa dimer. The AEL exhibits agglutinating activity against rabbit (74.41 UH/mP) and human type ABO erythrocytes (21.00 UH/mP). This activity does not require the presence of divalent cations and is specifically inhibited by lactose, fructose and mannose. The intravenous treatment with 0.01, 0.1 and 1 mg/kg of AEL inhibited the paw edema elicited by carrageenan by approximately 15, 22 and 44 %, respectively, but not that induced by dextran. In addition, treatment with 0.1, 1 and 10 mg/kg of AEL also inhibited the abdominal writhing induced by acetic acid by approximately 52, 57 and 69 %, respectively. In conclusion, AEL is a new lectin with a molecular mass of 20.0 kDa, which is -composed of a 10.291-Da monomer and a 20.582-kDa dimer, that exhibits anti-inflammatory, antinociceptive and hemagglutinating activities. In addition, the lectin hemagglutinating property is both metallo-independent and associated with the lectin domain.
Starting Page	674
Ending Page	680
Page Count	7
File Format	PDF
ISSN	15723887
Journal	The Protein Journal
Volume Number	31
Issue Number	8
e-ISSN	15734943
Language	English
Publisher	Springer US
Publisher Date	2012-09-11
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Plant lectin Abelmoschus esculentus Seeds Purification Anti-inflammatory Antinociceptive Biochemistry Bioorganic Chemistry Organic Chemistry Animal Anatomy / Morphology / Histology
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Analytical Chemistry Biochemistry Bioengineering

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