Expression of Adenylate Kinase 1 in Bovine Retinal Cytosol

• Published in: Current eye research Vol. 32; no. 3; pp. 249 - 257
• Main Authors: Ravera, Silvia, Musante, Luca, Calzia, Daniela, Panfoli, Isabella, Bruschi, Maurizio, Candiano, Giovanni, Pepe, Isidoro Mario, Morelli, Alessandro
• Format: Journal Article
• Language: English
• Published: England Informa UK Ltd 01.01.2007; Taylor & Francis
• Subjects: Adenylate kinase; Adenylate Kinase - isolation & purification; Adenylate Kinase - metabolism; Animals; Blotting, Western; Cattle; Chromatography, High Pressure Liquid; Chromatography, Ion Exchange; Cytosol - enzymology; Electrophoresis, Gel, Two-Dimensional; Electrophoresis, Polyacrylamide Gel; expression; Isoenzymes - isolation & purification; Isoenzymes - metabolism; Rabbits; Rats; retina; Retina - enzymology; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; two-dimensional electrophoresis
• ISSN: 0271-3683; 1460-2202
• DOI: 10.1080/02713680601161212

Adenylate kinases (AKs) are ubiquitous phosphotransferases that contribute to homeostasis of adenine nucleotide composition in cells. Six AK isoforms were found in vertebrates. We report that soluble AK isoform 1 is expressed in the cytosol of bovine retina consistently devoid of rod outer segments. Immunoblotting analysis with a polyclonal antibody raised against soluble adenylate kinase and subsequent sequencing of eluted peptide by matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry allowed enzyme isolation by joining purification methods to two-dimensional electrophoresis. In this study, we found that cytosolic adenylate kinase isoform 1 is expressed in bovine retina. Cytoplasmic AK1 would physiologically contribute to retinal energy metabolism.