Purification and properties of the hemagglutinin from Maclura pomifera seeds
- 1 December 1977
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 16 (26) , 5790-5794
- https://doi.org/10.1021/bi00645a023
Abstract
M. pomifera seeds contain a protein which agglutinates human erythrocytes at concentrations as low as 4 ng/ml. This property is related to its ability to bind with high specificity various .alpha.-D-galactopyranosides. The agglutinin, which was purified by affinity adsorption, exhibits 1 band on immunoelectrophoresis and displays 1 peak during ultracentrifugation, isoelectric focusing and gel permeation chromatography. The active protein has a MW of 40,000-43,000 and contains 2 dissimilar polypeptide chains of 12,000 and 10,000, respectively.This publication has 1 reference indexed in Scilit:
- The gel-filtration behaviour of proteins related to their molecular weights over a wide rangeBiochemical Journal, 1965