Abstract
Of the 10 precipitinogens present in the broth filtrate from yeast-phase cultures of Histoplasma capsulatum, none appeared to be nucleic acids because they were not inactivated by deoxyribonuclease or ribonuclease, four appeared to be proteins because they were inactivated by pepsin or trichloroacetic acid, and six appeared to be carbohydrates. The results of gel filtration chromatography suggested that the range of molecular weight of the antigens was from less than 50,000 for some of the carbohydrates to more than 200,000 for some of the proteins. By Sephadex and diethylaminoethyl cellulose chromatography and by the ultracentrifugation, two of the carbohydrate antigens, and one of the protein antigens were obtained in a form free of other antigens. When assayed by quantitative precipitation, the protein antigen and one of the carbohydrate antigens gave more precipitate at equivalence than did the whole filtrate. This finding indicates that whole filtrate contained inhibitors that could be removed by fractionation procedures.

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