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The N-acetylgalactosamine and lactosamine specific lectin from Iris hybrida leaves.
- Source :
-
Acta biochimica Polonica [Acta Biochim Pol] 1997; Vol. 44 (2), pp. 301-7. - Publication Year :
- 1997
-
Abstract
- The lectin isolated from the leaves of Iris hybrida binds specifically N-acetyl-galactosamine and lactose. Its molecule consists of two identical subunits bound by disulfide bonds. The lectin is a glycoprotein containing about 12% of sugars. It binds asialoglycoproteins containing complex type sugar chains. The binding is reduced by half at the concentration of 0.15 to 0.40 mM of the galactose containing disaccharides irrespectively to a type of galactose isomer. This indicates rather broad specificity of I. hybrida leaf lectin.
- Subjects :
- Disaccharides metabolism
Electrophoresis
Galactose metabolism
Glycoproteins metabolism
Lectins analysis
Plant Leaves chemistry
Plant Leaves metabolism
Plant Lectins
Plant Roots chemistry
Plant Roots metabolism
Plants metabolism
Substrate Specificity
Acetylgalactosamine metabolism
Amino Sugars metabolism
Lectins isolation & purification
Lectins metabolism
Plants chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0001-527X
- Volume :
- 44
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Acta biochimica Polonica
- Publication Type :
- Academic Journal
- Accession number :
- 9360719