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Binding of Helix Pomatia A Hemagglutinin to Human Erythrocytes and their Cells. Influence of Multivalent Interaction on Affinity
Author(s) -
HAMMARSTRÖM STEN
Publication year - 1973
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1973.tb02016.x
Subject(s) - hemagglutinin (influenza) , mole , helix pomatia , biology , binding constant , divalent , microbiology and biotechnology , cell culture , hemagglutination , biochemistry , chemistry , binding site , biophysics , virus , virology , snail , genetics , ecology , organic chemistry
The binding of 125 I‐labelled intact (hexavalent) and partially reduced (divalent) Helix pomatia A hemagglutinin to human A. 1 , A. 2 , A. 3 , A 1 B and A 2 B erythrocytes, human lymphocytes, human lymphoblastoid and other tumor cell lines was investigated. The essential finding was that the association constants calculated for the interaction between hemagglutinin and A‐erythrocytes were many orders of magnitude higher than the intrinsic association constant for the interaction between the hemagglutinin and the blood group A determinant. The latter value was 5–10 3 1/mole. The K‐values for intact hemagglutinin and A and AB erythrocytes were in the order of 10 10 1/mole at 18–22 °C and pH 7.3. For partially reduced hemagglutinin the K‐values were in the order of 5–10 7 1/mole. Multivalent interaction would seem to be the essential factor responsible for the high K‐values in the cell binding experiments. Intact hemagglutinin reacted against A 1 and A 2 erythrocytes or against a human osteogenic sarcoma cell tine (2T) gave homogeneous binding curves in Scatchard's plot. Human lymphocytes and most lymphoblastoid cell lines lacked hemagglutinin receptors.