Detection of Annexin IV in Bovine Retinal Rods

E. Yu. Zernii, N. K. Tikhomirova, P. P. Philippov^*, and I. I. Senin

Laboratory of Visual Reception, Department of Cell Signaling, Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119992 Russia; fax: (095) 939-0978; E-mail: ppph@belozersky.msu.ru

^* To whom correspondence should be addressed.

Received July 23, 2002; Revision received September 6, 2002

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The fraction of proteins capable of binding to photoreceptor membranes in a Ca²⁺-dependent manner was isolated from bovine rod outer segments. One of these proteins with apparent molecular mass of 32 kD (p32) was purified to homogeneity and identified as annexin IV (endonexin) by MALDI-TOF mass-spectrometry. In immunoblot, annexin IV purified from bovine rod outer segments cross-reacted with antibodies against annexin IV from bovine liver. This is the first detection of annexin IV in vertebrate retina.

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KEY WORDS: annexin IV, Ca²⁺-binding proteins, retinal rods, retina

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