Adenylate kinase activity in rod outer segments of bovine retina

Biochim Biophys Acta. 2001 Apr 2;1504(2-3):438-43. doi: 10.1016/s0005-2728(01)00160-8.


The rod outer segments of bovine retina contain two different adenylate kinases: a soluble activity, which is not sensitive to calcium ion, and an activity bound to disk membranes, which is dependent on the calcium levels. In fact, the maximal activity associated to the disks is reached at Ca(2+) concentrations between 10(-6) and 10(-7) M, which is the range of calcium level actually present in the rod cell. The Michaelis-Menten kinetics of the enzyme activity on disk membranes was determined and the actual concentrations of ATP, AMP and ADP were measured in the photoreceptor outer segment. Therefore, the physiological relevance of the adenylate kinase activity was discussed considering the above results. The formation of ATP catalyzed by the enzyme seems appropriate to supply at least some of the reactions necessary for phototransduction, indicating that ATP could be regenerated from ADP directly on the disk membranes where the photoreception events take place.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate / metabolism
  • Adenosine Triphosphate / metabolism
  • Adenylyl Cyclases / metabolism*
  • Animals
  • Calcium / metabolism
  • Calcium / pharmacology
  • Cattle
  • In Vitro Techniques
  • Light
  • Optic Disk / enzymology
  • Retina / enzymology*
  • Rod Cell Outer Segment / enzymology*


  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • Adenylyl Cyclases
  • Calcium