Abstract
To obtain the maximum yield of p-aminobenzoic acid (vitamin H'') from yeast, this was allowed to autolyse in a closed chamber before drying and extraction with acetone. Since in intact yeast, the acid appeared to be bound, perhaps with a peptide linkage to protein, the effect of combining it with various amino acids as peptide was investigated. As measured by the growth of Strep. plantarum, p-aminobenzoyl-1-glutamic acid as an antagonist to p-sulfanilamide was 8-10 times more active than an equimolecular amt. of p-aminobenzoic acid; similar peptides of d-glutamic acid, l-asparaginic ,acid, l-leucine, d-leucine, glycine and glycylglycine were inactive. The growth of the bacterium was much less strongly inhibited by unphysiological high doses of p-aminobenzoyl-1-glutamic acid than by corresponding doses of p-aminobenzoic acid.