Cyclic AMP-dependent protein kinase activity, subcellular distribution, and isozyme profile were compared in rabbit, rat, guinea pig, and mouse in both parotid and submandibular glands. Glands were homogenized under hypotonic conditions and the following fractions isolated: 600 g pellet, 27,000 g pellet, and 27,000 g supernatant. The specific activity of the enzyme was similar in the eight glands and was highest in the 27,000 g supernatant. The average activity in the 27,000 g supernatant was approximately 75% of the total gland activity, although there was considerable variability between tissues and species. After being washed with isotonic buffer, this percentage was increased to an average of 84%. When isozyme patterns of the kinase were examined, the rabbit parotid was unique in that it contained a high percentage of isozyme I as isolated on DEAE cellulose columns.
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