Аннотация:A number of different representatives of the annexin family has been detected and investigated in many mammalian tissues. However, only preliminary data have quite recently been published on the presence of annexins in mammalian retina. In this study, we purified a protein with an apparent molecular weight of 32 kDa from bovine rod outer segments (ROS) and identified it, by MALDI-TOF mass-spectrometry, as annexin IV. We also used a column with agarose-immobilized annexin IV to reveal soluble ROS proteins capable of binding to annexin IV in a Ca2+-dependent manner. These proteins which might be considered as potential targets of annexin IV include annexins II and VI as well as recoverin and creatine kinase. In addition, we investigated Ca2+- and Zn2+-dependent binding of annexin IV to urea-washed photoreceptor membranes and annexin IV-induced aggregation of the membranes.