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Abstract
Lysosomal hyaluronidase in the rabbit iris was studied by means of a sensitive assay method based on carbocyanine dye binding. The enzyme activity in the lysosomal extract was proportional to both the enzyme concentration and the incubation time. When the enzyme was heated, the enzyme activity was lost completely. When the lysosomal extract was used as an enzyme source, the enzyme activity was protected by pepstatin. The enzyme had a pH optimum of 3.8 and no activity above pH 5.0.