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Influence of mannan epitopes in glycoproteins - Concanavalin A interaction. Comparison of natural and synthetic glycosylated proteins

Mislovicova, D; Masarova, J; Svitel, Juraj LU and Gemeiner, P (2002) In International Journal of Biological Macromolecules 30(5). p.251-258
Abstract
Two natural glycoproteins/glycoenzymes, invertase and glucoamylase, and two neoglycoconjugates, synthetized from Saccharomyces cerevisiae mannan, bovine serum albumin and penicillin G acylase were tested for interaction with lectin Concanavalin A (Con A). The interaction of natural and synthetic glycoproteins with Con A was studied using three different experimental methods: (i) quantitative precipitation in solution (ii) sorption to Con A immobilized on bead cellulose; and (iii) kinetic measurement of the interaction by surface plasmon resonance. Prepared neoglycoproteins were further characterized: saccharide content, molecular weight, polydispersion, kinetic and equilibrium association constants with Con A were determined. It can be... (More)
Two natural glycoproteins/glycoenzymes, invertase and glucoamylase, and two neoglycoconjugates, synthetized from Saccharomyces cerevisiae mannan, bovine serum albumin and penicillin G acylase were tested for interaction with lectin Concanavalin A (Con A). The interaction of natural and synthetic glycoproteins with Con A was studied using three different experimental methods: (i) quantitative precipitation in solution (ii) sorption to Con A immobilized on bead cellulose; and (iii) kinetic measurement of the interaction by surface plasmon resonance. Prepared neoglycoproteins were further characterized: saccharide content, molecular weight, polydispersion, kinetic and equilibrium association constants with Con A were determined. It can be concluded that the used conjugation method proved to be able to produce neoglycoproteins with similar properties like natural glycoproteins, i.e. enzymatic activity (protein part) and lectin binding activity (mannan part) were preserved and the neoglycoconjugates interact with Con A similarly as natural mannan-type glycoproteins. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
lectin-polysaccharide interaction, Concanavalin A, neoglycoproteins, mannan, glycosylated enzymes, immobilization of neoglycoenzymes
in
International Journal of Biological Macromolecules
volume
30
issue
5
pages
251 - 258
publisher
Elsevier
external identifiers
  • pmid:12297232
  • wos:000178651500005
  • scopus:0036803925
ISSN
1879-0003
DOI
10.1016/S0141-8130(02)00035-1
language
English
LU publication?
yes
id
4bfd8c22-873d-4359-861c-98d64d4ce100 (old id 325711)
date added to LUP
2007-11-16 14:44:28
date last changed
2017-01-01 05:04:42
@article{4bfd8c22-873d-4359-861c-98d64d4ce100,
  abstract     = {Two natural glycoproteins/glycoenzymes, invertase and glucoamylase, and two neoglycoconjugates, synthetized from Saccharomyces cerevisiae mannan, bovine serum albumin and penicillin G acylase were tested for interaction with lectin Concanavalin A (Con A). The interaction of natural and synthetic glycoproteins with Con A was studied using three different experimental methods: (i) quantitative precipitation in solution (ii) sorption to Con A immobilized on bead cellulose; and (iii) kinetic measurement of the interaction by surface plasmon resonance. Prepared neoglycoproteins were further characterized: saccharide content, molecular weight, polydispersion, kinetic and equilibrium association constants with Con A were determined. It can be concluded that the used conjugation method proved to be able to produce neoglycoproteins with similar properties like natural glycoproteins, i.e. enzymatic activity (protein part) and lectin binding activity (mannan part) were preserved and the neoglycoconjugates interact with Con A similarly as natural mannan-type glycoproteins.},
  author       = {Mislovicova, D and Masarova, J and Svitel, Juraj and Gemeiner, P},
  issn         = {1879-0003},
  keyword      = {lectin-polysaccharide interaction,Concanavalin A,neoglycoproteins,mannan,glycosylated enzymes,immobilization of neoglycoenzymes},
  language     = {eng},
  number       = {5},
  pages        = {251--258},
  publisher    = {Elsevier},
  series       = {International Journal of Biological Macromolecules},
  title        = {Influence of mannan epitopes in glycoproteins - Concanavalin A interaction. Comparison of natural and synthetic glycosylated proteins},
  url          = {http://dx.doi.org/10.1016/S0141-8130(02)00035-1},
  volume       = {30},
  year         = {2002},
}