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The NH2 terminus of retinal recoverin is acylated by a small family of fatty acids.
Open accessAbstract
Recoverin is a recently identified Ca(2+)-binding protein that imparts Ca2+ sensitivity to vertebrate photoreceptor guanylate cyclase. In response to photo-induced depletion of intracellular cGMP and Ca2+, recoverin stimulates resynthesis of cGMP. Bovine retinal recoverin has now been analyzed by electrospray mass spectrometry (ESI-MS) for post-translational modifications that might influence its activity. Heterogeneous acylation was detected at the NH2 terminus of bovine retinal recoverin. The NH2-terminal glycine of each retinal recoverin molecule is linked to one of four different types of acyl groups. The most abundant is myristoleate (14:1), but 14:0, 14:2, and 12:0 acyl residues are also present.
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Metadata
- Authors
- Dizhoor, A. M., Ericsson, L. H., Johnson, R. S., Kumar, S., Olshevskaya, E., Zozulya, S., Neubert, T. A., Stryer, L., Hurley, J. B., & Walsh, K. A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1992-08
- Volume
- 267
- Issue
- 23
- Pages
- 16033-16036
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1536183747
- Cited by
- 215
- References
- 0
- FWCI
- 25.63
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Dizhoor, A. M., Ericsson, L. H., Johnson, R. S., Kumar, S., Olshevskaya, E., Zozulya, S., Neubert, T. A., Stryer, L., Hurley, J. B., & Walsh, K. A. (1992). The NH2 terminus of retinal recoverin is acylated by a small family of fatty acids. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)41959-x
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