Protein-carbohydrate interaction I. The interaction of polysaccharides with concanavalin A

The precipitin reaction between concanavalin A, a globulin isolated from jackbean meal, and certain polysaccharides has been examined. Using a turbidimetric assay and a partially purified concanavalin A preparation, it has been shown that only branched polysaccharides possessing α- d-glucopyranosyl...

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Published inBiochimica et biophysica acta Vol. 97; no. 1; pp. 68 - 76
Main Authors Goldstein, I.J., Hollerman, C.E., Merrick, J.M.
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 04.01.1965
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Abstract The precipitin reaction between concanavalin A, a globulin isolated from jackbean meal, and certain polysaccharides has been examined. Using a turbidimetric assay and a partially purified concanavalin A preparation, it has been shown that only branched polysaccharides possessing α- d-glucopyranosyl or α- d-mannopyranosyl units will interact with the protein to form a precipitate. The extent of precipitate formation is dependent on the concentration of both concanavalin A and polysaccharide and the reaction appears to be analogous to an antibody-antigen system. The frequency of branching of the polysaccharide molecule plays an important role in the extent of interaction with concanavalin A. Dextrans may be classified according to their extent of reaction with the protein.
AbstractList The precipitin reaction between concanavalin A, a globulin isolated from jackbean meal, and certain polysaccharides has been examined. Using a turbidimetric assay and a partially purified concanavalin A preparation, it has been shown that only branched polysaccharides possessing α- d-glucopyranosyl or α- d-mannopyranosyl units will interact with the protein to form a precipitate. The extent of precipitate formation is dependent on the concentration of both concanavalin A and polysaccharide and the reaction appears to be analogous to an antibody-antigen system. The frequency of branching of the polysaccharide molecule plays an important role in the extent of interaction with concanavalin A. Dextrans may be classified according to their extent of reaction with the protein.
Author Goldstein, I.J.
Merrick, J.M.
Hollerman, C.E.
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  surname: Merrick
  fullname: Merrick, J.M.
BackLink https://www.ncbi.nlm.nih.gov/pubmed/14284321$$D View this record in MEDLINE/PubMed
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Issue 1
Keywords PLANT PROTEINS
PRECIPITIN TESTS
BIOCHEMISTRY
LIVER GLYCOGEN
DEXTRAN
EXPERIMENTAL LAB STUDY
POLYSACCHARIDES
SACCHAROMYCES
GLOBULINS
Language English
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elsevier_sciencedirect_doi_10_1016_0304_4165_65_90270_9
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PublicationDate 1965-01-04
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PublicationDecade 1960
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PublicationTitle Biochimica et biophysica acta
PublicationTitleAlternate Biochim Biophys Acta
PublicationYear 1965
Publisher Elsevier B.V
Publisher_xml – name: Elsevier B.V
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  ident: 10.1016/0304-4165(65)90270-9_BIB30
  article-title: Lectures in Immunochemistry
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Snippet The precipitin reaction between concanavalin A, a globulin isolated from jackbean meal, and certain polysaccharides has been examined. Using a turbidimetric...
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SubjectTerms Biochemical Phenomena
Biochemistry
Concanavalin A
Dextrans
Globulins
Liver Glycogen
OldMedline
Plant Proteins
Polysaccharides
Precipitin Tests
Saccharomyces
Title Protein-carbohydrate interaction I. The interaction of polysaccharides with concanavalin A
URI https://dx.doi.org/10.1016/0304-4165(65)90270-9
https://www.ncbi.nlm.nih.gov/pubmed/14284321
https://www.proquest.com/docview/83994799
Volume 97
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