Multiple soluble beta-galactoside-binding lectins from human lung.

Abstract

Soluble extracts of human lung contain three major beta-galactoside-binding proteins with apparent subunit molecular weights of 14,000 (HL-14), 22,000 (HL-22), and 29,000 (HL-29). HL-14 and HL-29 were abundant in all the specimens that we tested whereas HL-22 was abundant in some and very scarce in others. HL-14 could be resolved into at least six acidic forms by isoelectric focusing and HL-29 into at least five acidic forms by this procedure. In contrast, HL-22 is a basic protein. Other beta-galactoside-binding proteins with subunit molecular weights ranging from about 16,000 to 27,000 were also detected in lung extracts, but the possibility that they are degradation products cannot be excluded. HL-14 is very similar to a rat lung lectin (RL-14.5) in carbohydrate binding specificity and amino acid composition and reacts strongly with an antiserum raised against the rat lectin. HL-29 is similar to the rat lectin RL-29 in the same respects, but its carbohydrate binding specificity is somewhat different. Of the known rat lectins, HL-22 resembles RL-18 most closely in carbohydrate binding specificity, but it is significantly different in other properties and does not react with an antiserum raised against the rat lectin.