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A Diocleinae type II lectin from Dioclea lasiophylla Mart. Ex Benth seeds specific to alpha-lactose/GalNAc
- Source :
- PROCESS BIOCHEMISTRY
- Publication Year :
- 2020
-
Abstract
- A type II lectin, designated as DlyL2, was purified from Dioclea lasiophylla Mart. ex Benth seeds and some of its physicochemical properties determined. The lectin demonstrated specificity for α-lactose and N-acetyl- d -galactosamine and was able to interact with porcine stomach mucin. DlyL2 has 0.78 % carbohydrates in its composition, therefore can be considered a glycoprotein. In addition, its hemagglutinating activity remained stable at a temperature of 90 °C and in a pH range from 5 to 10. Metal chelation treatment did not affect DlyL2 activity suggesting it's not a metalloprotein. Dlyl2 showed an apparent mass of 31 kDa and average molecular mass of 26.371 kDa. Primary structure data could be generated from the partial amino acid sequence of DlyL2, with about 192 residues sequenced by a combination of Edman degradation and tandem mass spectrometry. The lectin is similar to other type II lectins from Diocleinae subtribe, as well as lectins derived from species of more ancient tribes of the Fabaceae family. In addition, DlyL2 exhibited no toxicity to Artemia sp. nauplii. The present study expands the knowledge about the specificity, structural and physicochemical properties of Diocleinae type II lectins.
- Subjects :
- 0106 biological sciences
CANAVALIA-MARITIMA
Diocleinae
PROTEIN
Bioengineering
MANNOSE-SPECIFIC LECTIN
Tandem mass spectrometry
01 natural sciences
Applied Microbiology and Biotechnology
Biochemistry
SEQUENCE
GALACTOSE
03 medical and health sciences
chemistry.chemical_compound
010608 biotechnology
Metalloprotein
Peptide sequence
030304 developmental biology
chemistry.chemical_classification
0303 health sciences
CARBOHYDRATE-BINDING
PURIFICATION
Molecular mass
biology
Edman degradation
Type II lectin
Chemistry
Protein primary structure
Lectin
Dioclea lasiophylla
IMMOBILIZATION
Galactosamine
biology.protein
Subjects
Details
- Language :
- English
- ISSN :
- 13595113 and 18733298
- Database :
- OpenAIRE
- Journal :
- PROCESS BIOCHEMISTRY
- Accession number :
- edsair.doi.dedup.....e68a708109249a640fd5669b01eb0a87