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Open AccessJournal ArticleDOI

Identification of the Blood‐Group ABH‐Active Glycoprotein Components of Human Erythrocyte Membrane

Jukka Finne
- 01 Feb 1980 - 
- Vol. 104, Iss: 1, pp 181-189
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TLDR
The different lectin-binding properties indicate a structural difference between the antigenic determinants of the sialoglycoproteins and of the other blood-group-active components, which could explain the controversy concerning the nature of the blood- group ABH antigens in glycoprotein of the erythrocyte membrane.
Abstract
The blood-group ABH-active components of the erythrocyte membrane were identified by incubation of polyacrylamide gels after electrophoresis with radio-iodinated blood-group-specific lectins. The anti-A and anti-B lectin of Bandeiraea simplicifolia bound to components from A1, AB and B erythrocytes but not A2 or O erythrocytes, whereas the opposite was observed for the anti-H lectin of Lotus tetragonolobus. Both lectins revealed as major blood-group-active components band 3 and the region of band 4.5, which was resolved into at least two components. Smaller amounts of the lectins were bound to the low-molecular-weight region and the dye front, which contained the poly(glycosyl)ceramides. In addition to these components, the B. simplicifolia lectin also bound to the sialoglycoprotein bands 1 and 2 (stained with periodic acid/Schiff). The distribution of bound radioactivity, as determined with this lectin was: Band 3, 22–25%; HIO4/Schiff band-1, 10–15%; band 4.5, 34–37%; HIO4/Schiff band-2, 12–15%; and the poly(glycosyl)ceramide region, 14–17%. The different lectin-binding properties indicate a structural difference between the antigenic determinants of the sialoglycoproteins and of the other blood-group-active components. It is suggested that the antigenic determinants in the sialoglycoproteins are of the alkali-labile type previously characterized, and that the carbohydrate chains of bands 3 and 4.5 correspond to the previously isolated alkali-stable poly(glycosyl)peptides. The detection of two different groups of glycoproteins could thus explain the controversy concerning the nature of the blood-group ABH antigens in glycoproteins of the erythrocyte membrane.

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Citations
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Journal ArticleDOI

Identification of the O-linked sialyloligosaccharides of glycophorin A as the erythrocyte receptors for S-fimbriated Escherichia coli.

TL;DR: Results indicated that the major erythrocyte receptor for S-fimbriated E. coli is the NeuAc alpha 2-3Gal beta 1-3 GalNAc sequence of the O-linked oligosaccharide chains of glycophorin A.
Journal ArticleDOI

Escherichia coli strains binding neuraminyl α2–3 galactosides

TL;DR: Nine E. coli strains showing mannose-resistant, P-blood-group independent hemagglutination of human erythrocytes were tested for binding to neuraminic acid and showed binding specificity for α2–3 linked neuraminimic acid.
Book ChapterDOI

Preparation and fractionation of glycopeptides.

Jukka Finne, +1 more
TL;DR: The double extraction procedure with chloroform-methanol 2:1 and 1:2 has been widely used and has the advantage that even the highly glycosylated glycolipids (polyglycosyl ceramides H) become solubilized, and most glycoproteins remain insoluble.
Journal ArticleDOI

ABO-incompatible kidney transplantation.

TL;DR: The hypothesis is reached that the structural difference of ABO histo-blood group antigens and de novo corresponding antibody production would be the key and keyhole of the development of acute AMR in ABOI-KTx.
References
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Journal ArticleDOI

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article

Cleavage of structural proteins during the assemble of the head of bacterio-phage T4

U. K. Laemmli
- 01 Jan 1970 - 
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
Journal ArticleDOI

The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis

TL;DR: The results show that the polyacrylamide gel electrophoresis method can be used with great confidence to determine the molecular weights of polypeptide chains for a wide variety of proteins.
Journal ArticleDOI

The preparation of 131i-labelled human growth hormone of high specific radioactivity

TL;DR: The loss of immunological reactivity at high specific radioactivities or at high levels of chemical substitution with STAI/sup 127/!iodine is demonstrated.
Journal ArticleDOI

A Film Detection Method for Tritium‐Labelled Proteins and Nucleic Acids in Polyacrylamide Gels

TL;DR: A simple method for detecting 3H in polyacrylamide gels by scintillation autography (fluorography) using X-ray film, which is ten times more sensitive than conventional autoradiography of isotopes with higher emission energies.
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