Abstract
We isolated two types of protein kinase C-related enzymes (fPKC) in frog ( Rana catesbeiana) retina. Three sequential steps of column chromatography of DEAE-cellulose, butyl-Toyopearl, and hydroxylapatite were carried out and resulted in the separation of two types of distinct Ca 2+/phospholipid-dependent protein kinase activities. These proteins reacted with antibodies raised against synthetic peptides based on the predicted amino acid sequences of rat protein kinase C δ or ζ subspecies, and showed molecular masses of 90 and 75 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, respectively. Immunocytochemical analysis of 90 and 75K fPKC in frog retina revealed that the 75K fPKC was localized in the outer segment of cone cells and in the microvillar projections of Müller cells, and that 90K fPKC was mainly distributed in Müller cells. These results suggested that fPKCs play differential roles on the photosignal transduction in frog retina.
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