lectin-binding sites of the erythrocyte membrane components of horse, swine and sheep. Characterization by their molecular weights

The membrane components of equine, porcine and ovine erythrocytes were separated by sodium dodecylsulfate polyacrylamide gel electrophoresis and subsequently incubated with the radioiodinated lectins from lentils (LCH), castorbeans (RCA), Phaseolus beans (L-PHA), gorse seeds (UEH-F) and from vineyar...

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Bibliographic Details
Published inHoppe-Seyler's Zeitschrift für Physiologische Chemie Vol. 360; no. 3; pp. 421 - 428
Main Authors Gurtler, L.G, Yeboa, D.A, Cleve, H
Format Journal Article
LanguageEnglish
Published Germany 01.03.1979
Subjects
animal science
Animals
Erythrocyte Membrane - ultrastructure
Erythrocytes - ultrastructure
Hemagglutination
Horses
Humans
Lectins
livestock
Membrane Proteins - blood
Molecular Weight
Sheep
Species Specificity
Swine
zoology
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Summary:The membrane components of equine, porcine and ovine erythrocytes were separated by sodium dodecylsulfate polyacrylamide gel electrophoresis and subsequently incubated with the radioiodinated lectins from lentils (LCH), castorbeans (RCA), Phaseolus beans (L-PHA), gorse seeds (UEH-F) and from vineyard snails (HPA). The following individual glycoproteins could be labeled: gp 26, 33, 100 and 320 in horse erythrocytes, gp 24, 46, 75, 130 and 210 in swine and gp 24, 57, 100 and 210 in sheep erythrocytes.
ISSN:0018-4888