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Structural characterization of novel chitin-binding lectins from the genus Artocarpus and their antifungal activity
- Source :
- Biochimica et biophysica acta. 1764(1)
- Publication Year :
- 2005
-
Abstract
- Two novel chitin-binding lectins from seeds of Artocarpus genus were described in this paper, one from A. integrifolia (jackfruit) and one from A. incisa (breadfruit). They were purified from saline crude extract of seeds using affinity chromatography on chitin column, size-exclusion chromatography and reverse-phase chromatography on the C-18 column. Both are 14 kDa proteins, made up of 3 chains linked by disulfide bonds. The partial amino acid sequences of the two lectins showed they are homologous to each other but not to other plant chitin-binding proteins. Thus, they cannot be classified in any known plant chitin-binding protein family, particularly because of their inter-chain covalent bonds. Their circular dichroism spectra and deconvolution showed a secondary structure content of beta-sheet and unordered elements. The lectins were thermally stable until 80 degrees C and structural changes were observed below pH 6. Both lectins inhibited the growth of Fusarium moniliforme and Saccharomyces cerevisiae, and presented hemagglutination activity against human and rabbit erythrocytes. These lectins were denoted jackin (from jackfruit) and frutackin (from breadfruit).
- Subjects :
- Circular dichroism
Antifungal Agents
Molecular Sequence Data
Biophysics
Chitin
Biology
In Vitro Techniques
Biochemistry
Protein Structure, Secondary
Analytical Chemistry
Artocarpus
chemistry.chemical_compound
Protein structure
Affinity chromatography
Fusarium
Chitin binding
Spectroscopy, Fourier Transform Infrared
Animals
Humans
Amino Acid Sequence
Molecular Biology
Protein secondary structure
chemistry.chemical_classification
Sequence Homology, Amino Acid
Circular Dichroism
Hemagglutination Tests
biology.organism_classification
Amino acid
Spectrometry, Fluorescence
chemistry
Aspergillus niger
Rabbits
Plant Lectins
Protein Binding
Subjects
Details
- ISSN :
- 00063002
- Volume :
- 1764
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Biochimica et biophysica acta
- Accession number :
- edsair.doi.dedup.....cee2904ee4ddb92adc5d91958d2102d2