Abstract
A simple procedure for isolation of lysosomes from rat salivary gland was developed. The highest activity for succinate dehydrogenase was found in the 4, 000×g pellet (F-2), the highest activity for acid phosphatase in the 20, 000×g pellet (F-3), and the highest activity for acid DNase in both the 20, 000×g pellet (F-3) and the 4, 000×g pellet (F-2). Acid DNase was extracted from the 20, 000×g pellet (F-3) by treatment with Triton X-100. There were no differences in the proportions or migration patterns in acid DNase for the 20, 000×g pellet (F-3) and the 20, 000×g supernatant (F-4) as observed on pH 4.3 electrophoresed gels. On the pH 8.8 gel, acid DNase from the 20, 000×g supernatant (F-4) yielded a distinct single band; however this band was absent from the 20, 000×g pellet (F-3).
