NDLI: Purification and primary structure of a mannose/glucose-binding lectin from Parkia biglobosa Jacq. seeds with antinociceptive and anti-inflammatory properties.

Please wait, while we are loading the content...

Purification and primary structure of a mannose/glucose-binding lectin from Parkia biglobosa Jacq. seeds with antinociceptive and anti-inflammatory properties.

A systematic method for analysing the protein hydration structure of T4 lysozyme.

A biophysical characterization of the folded domains of KCTD12: insights into interaction with the GABAB2 receptor.

Behavior of human immunoglobulin G adsorption onto immobilized Cu(II) affinity hollow-fiber membranes.

Year: 2013 Volume: 26 Issue: 9

Year: 2013 Volume: 26 Issue: 8

Year: 2013 Volume: 26 Issue: 7

Year: 2013 Volume: 26 Issue: 6

Year: 2013 Volume: 26 Issue: 5

Year: 2013 Volume: 26 Issue: 4

Year: 2013 Volume: 26 Issue: 3

Year: 2013 Volume: 26 Issue: 2

Year: 2013 Volume: 26 Issue: 1

Year: 2012 Volume: 25

Year: 2011 Volume: 24

Year: 2010 Volume: 23

Year: 2009 Volume: 22

Year: 2008 Volume: 21

Year: 2007 Volume: 20

Year: 2006 Volume: 19

Year: 1989 Volume: 2

Purification and primary structure of a mannose/glucose-binding lectin from Parkia biglobosa Jacq. seeds with antinociceptive and anti-inflammatory properties.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Silva, Helton C. Bari, Alfa U. Rocha, Bruno Anderson M. Nascimento, Kyria S. Ponte, Edson L. Pires, Alana F. Delatorre, Plínio Teixeira, Edson H. Debray, Henri Assreuy, Ana Maria S. Nagano, Celso S. Cavada, Benildo S.
Description	Country affiliation: Brazil Author Affiliation: Silva HC ( BioMol-Group, Department of Biochemistry and Molecular Biology, Federal University of Ceará, PO Box 6043, 60440-970, Fortaleza, CE, Brazil.)
Abstract	Parkia biglobosa (subfamily Mimosoideae), a typical tree from African savannas, possess a seed lectin that was purified by combination of ammonium sulfate precipitation and affinity chromatography on a Sephadex G-100 column. The P. biglobosa lectin (PBL) strongly agglutinated rabbit erythrocytes, an effect that was inhibited by d-mannose and d-glucose-derived sugars, especially -methyl-d-mannopyranoside and N-acetyl-d-glucosamine. The hemagglutinating activity of PBL was maintained after incubation at a wide range of temperature and pH and also was independent of divalent cations. By sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis, PBL exhibited an electrophoretic profile consisting of a single band with apparent molecular mass of 45 kDa. An analysis using electrospray ionization-mass spectrometry indicated that purified lectin possesses a molecular average mass of 47 562 ± 4 Da, and the analysis by gel filtration showed that PBL is a dimer in solution. The complete amino acid sequence of PBL, as determined using tandem mass spectrometry, consists of 443 amino acid residues. PBL is composed of a single non-glycosylated polypeptide chain of three tandemly arranged jacalin-related domains. Sequence heterogeneity was found in six positions, indicating that the PBL preparations contain highly homologous isolectins. PBL showed important antinociceptive activity associated to the inhibition of inflammatory process.
File Format	HTM / HTML
ISSN	09523499
Issue Number	10
Volume Number	26
e-ISSN	10991352
Journal	Journal of Molecular Recognition
Language	English
Publisher	Wiley
Publisher Date	2013-10-01
Publisher Place	Great Britain (UK)
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Molecular Biology Analgesics Isolation & Purification Anti-inflammatory Agents, Non-steroidal Fabaceae Chemistry Pain Drug Therapy Peritonitis Plant Lectins Acetic Acid Amino Acid Sequence Pharmacology Animals Carrageenan Cell Count Chromatography, Affinity Hemagglutination Tests Hydrogen-ion Concentration Mice Molecular Sequence Data Molecular Weight Monocytes Drug Effects Pathology Neutrophils Chemically Induced Physiopathology Protein Multimerization Protein Structure, Tertiary Rabbits Seeds Temperature Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Structural Biology Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Purification and primary structure of a novel mannose-specific lectin from Centrolobium microchaete Mart seeds.

Aqueous extract of Parkia biglobosa (Jacq.) R. Br. (Fabaceae) exerts antiepileptogenic, anti-amnesic, and anxiolytic-like effects in mice via mechanisms involving antioxidant and anti-inflammatory pathways

Purification, partial characterization and preliminary X-ray diffraction analysis of a mannose-specific lectin from Cymbosema roseum seeds.

Purification and partial characterization of a new mannose/glucose-specific lectin from Dialium guineense Willd seeds that exhibits toxic effect.

Anti-inflammatory and antinociceptive activity of chitin-binding lectin from Canna limbata seeds.

Purification and characterization of a mannose/N-acetyl-D-glucosamine-specific lectin from the seeds of Platymiscium floribundum Vogel.

Purification and biological activities of Abelmoschus esculentus seed lectin.

The first trimeric Galanthus nivalis agglutinin-related lectin of Orchidaceae was found in Dendrobium pendulum: purification, characterization, and effects of stress factors.

Purification, characterization and partial sequence of a pro-inflammatory lectin from seeds of Canavalia oxyphylla Standl. & L. O. Williams.

Purification and primary structure of a mannose/glucose-binding lectin from Parkia biglobosa Jacq. seeds with antinociceptive and anti-inflammatory properties.

Similar Documents

Purification and primary structure of a novel mannose-specific lectin from Centrolobium microchaete Mart seeds.

Aqueous extract of Parkia biglobosa (Jacq.) R. Br. (Fabaceae) exerts antiepileptogenic, anti-amnesic, and anxiolytic-like effects in mice via mechanisms involving antioxidant and anti-inflammatory pathways

Purification, partial characterization and preliminary X-ray diffraction analysis of a mannose-specific lectin from Cymbosema roseum seeds.

Purification and partial characterization of a new mannose/glucose-specific lectin from Dialium guineense Willd seeds that exhibits toxic effect.

Anti-inflammatory and antinociceptive activity of chitin-binding lectin from Canna limbata seeds.

Purification and characterization of a mannose/N-acetyl-D-glucosamine-specific lectin from the seeds of Platymiscium floribundum Vogel.

Purification and biological activities of Abelmoschus esculentus seed lectin.

The first trimeric Galanthus nivalis agglutinin-related lectin of Orchidaceae was found in Dendrobium pendulum: purification, characterization, and effects of stress factors.

Purification, characterization and partial sequence of a pro-inflammatory lectin from seeds of Canavalia oxyphylla Standl. & L. O. Williams.

Purification and primary structure of a mannose/glucose-binding lectin from Parkia biglobosa Jacq. seeds with antinociceptive and anti-inflammatory properties.