Issue 12, 2003

Studies on adenylate kinase isoform bound to disk membranes of the rod outer segment of bovine retina

Abstract

An adenylate kinase (AK) activity modulated by calcium ion concentration has been found associated to the disk membranes of the rod outer segment of bovine retina. A maximum activity of about 80 nmol ATP produced per min per mg protein was found at physiological calcium concentrations. Preliminary experiments suggest that the membrane binding is presumably promoted by fatty acylation of the protein. In fact, a protein with a molecular weight corresponding to the disk adenylate kinase was recognized by a polyclonal antiserum against the first 15 N-terminal amino acids of AK1β, a membrane-associated isoform of adenylate kinase, which belongs to the N-terminus myristoylated protein family. The adenylate kinase activity was also measured directly on the protein band transferred to nitrocellulose by Western blot.

Graphical abstract: Studies on adenylate kinase isoform bound to disk membranes of the rod outer segment of bovine retina

  • This article is part of the themed collection: Vision

Article information

Article type
Paper
Submitted
16 Dec 2002
Accepted
16 Jun 2003
First published
01 Jul 2003

Photochem. Photobiol. Sci., 2003,2, 1299-1302

Studies on adenylate kinase isoform bound to disk membranes of the rod outer segment of bovine retina

L. Notari, A. Morelli and I. M. Pepe, Photochem. Photobiol. Sci., 2003, 2, 1299 DOI: 10.1039/B306774M

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