Five structurally related proteins from affinity-purified Maclura pomifera lectin
- 1 April 1981
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 20 (9) , 2618-2620
- https://doi.org/10.1021/bi00512a039
Abstract
Affinity-purified M. pomifera lectin (MPL) elutes from a gel filtration column as a single symmetrical peak with characteristics expected for a single protein of .apprx. 40,000 daltons. This material can be dissociated into 2 dissimilar polypeptide chains of .apprx. 10,000 daltons. Ion-exchange chromatography on DEAE-cellulose resolves affinity-purified MPL into 5 components. These proteins are structurally related and contain varying proportions of the 2 polypeptide chains. Two of these tetrameric lectins, each composed solely of 1 of these chains, display differences in mobility during discontinuous polyacrylamide gel electrophoresis and ion-exchange chromatography but display no detectable differences in hemagglutination of human erythrocytes and interactions with carbohydrates.This publication has 6 references indexed in Scilit:
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