Abstract
A novel protein kinase activity was characterized from the cytosolic fraction of isolated rabbit gastric glands. The kinase phosphorylated a major 33,000 Da endogenous protein (pp33) and was stimulated by Zn 2+ and Mn 2+ with K act of 1.0 and 7.5 mM, respectively. Mg 2+ and Ca 2+ failed to stimulate any pp33 kinase activity. The kinase utilized both ATP and GTP as phosphate donors with a K m of 10 uM for both. The pp33 protein displayed an isoelectric point of 7.5 to 7.8 and was phosphorylated predominantly on threonine residues. The kinase activity is clearly differentiable from all reported kinase activities and appeared to be enriched in rabbit gastric fundic mucosa. The results indicate that gastric fundic mucosa contains a novel protein kinase activity.
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