Human airway lysozyme (HAL) was separated into fractions of distinct molecular forms using a Mono S cation-exchange column on a fast-protein liquid chromatography system. This new and rapid (30 min) purification procedure of human lysozyme enabled the preparation of fractions, highly enriched in different isoenzymes of HAL. Purified HAL from pathological purulent airway secretions, nonpurulent airway secretions, and normal tracheobronchial tissue culture medium was characterized by four, three, and only one enzymatically active molecular forms, respectively. All charge forms (separated or combined) recovered from either purulent or nonpurulent airway secretions or tracheobronchial culture medium exhibited the same apparent molecular weight of 15,000.
Chromatography, Ion Exchange Isoenzymes