Purification and Characterization of a Hemagglutinin from Arachis hypogaea
- 1 January 1975
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 356 (2) , 1685-1692
- https://doi.org/10.1515/bchm2.1975.356.2.1685
Abstract
A. hypogaea hemagglutinin was purified by (NH4)2 SO4 fractionation and Sepharose 6 B column chromatography. The homogeneity of the purified hemagglutinin was ascertained by ultracentrifugal analysis and polyacrylamide gel electrophoresis. It has a MW of 106,500 and is a tetramer of a subunit with a MW of 27,000. The purified hemagglutinin agglutinated neuraminidase-treated human erythrocytes regardless of their ABO group type, but did not agglutinate intact erythrocytes. In hapten inhibition assays with simple sugars, the so-called Makela''s group 2 sugars, which bear the same configuration of hydroxy groups at C-3 and C-4 as D-galactopyranose, were inhibitors for this hemagglutinin. It does not contain any carbohydrate, in contrast to most phytohemagglutinins except Concanavalin A and wheat germ agglutinin.This publication has 1 reference indexed in Scilit:
- THE OXIDATION OF RIBONUCLEASE WITH PERFORMIC ACIDJournal of Biological Chemistry, 1956