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      Identification and Partial Purification of a Nucleotide-Stimulated Protease in Rat Retina

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          A nucleotide-stimulated protease of rat retina was partially purified by DEAE-cellulose column chromatography. A 50-fold increase of an ATP-stimulated protease activity over a cytosol fraction was achieved by this chromatography. Maximum stimulation of protease activity by ATP was achieved at 2 mM. The pH optimum of the ATP-stimulated protease activity was between 7.5 and 8.5. 2 mM GTP stimulated the protease activity by 91%. 5 mM cyclic AMP stimulated the protease activity by 73% while 5 mM cyclic GMP stimulated the activity by 84%. The possible role of the nucleotide-stimulated protease in retina and potential involvement of the protease with inherited retinal dystrophy are discussed.

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          Author and article information

          Ophthalmic Res
          Ophthalmic Research
          S. Karger AG
          04 December 2009
          : 17
          : 5
          : 282-288
          Department of Ophthalmology and Visual Sciences, and Department of Pharmacology, Texas Tech University Health Sciences Center, Lubbock, Tex., USA
          265387 Ophthalmic Res 1985;17:282–288
          © 1985 S. Karger AG, Basel

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          Pages: 7
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