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By Felix Bronner

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METHODS Isolated RBC membranes w e r e prepared in 20 mM imidazole buffer from outdated blood as described by Farrance and Vin­ cenzi (1977a). 5 m l . , 1979) and was iodinated according to the method 7of LaPorte and Storm (1978), to a specific activity of 8 χ 1 0 CPM/nmole. Azido-CaM and azido-125i_çaM were prepared as described by Andreasen et al. (1981) with incorporation of one azido group per mole CaM. 2 mM EGTA. The mixture was then diluted with an equal volume of ice cold buffer and centrifuged in an Eppendorf Model 5412 Microcentrifuge for 5 min.

The sole function of Ca 2+ within the cytosol 1s to transmit information. The targets of Ca 2+, functioning as a second messenger, are proteins in the cytosol. Calcium-modulated proteins are homologous to one another and contain EF-hand domains. Cells initially extruded calcium to utilize phosphate as their basic energy currency; Ca 3 (P0 4 )2 is insoluble. Calmodulin is the prototype of calcium modulated proteins. We infer, from its presence in plants, fungi, tetrahymena, and various vertebrate tissues, that it is present in the cytosol of all (or most) cells of all (or most) eukaryotes.

01M Mg2+. SOME GENERAL COMMENTS S-100 can be said to be a further example of one type of calcium-binding protein - the calmodulins which change con­ formation on binding calcium, but are either not affected by T are altered by it in a different way. Using magnesium or K r e t s i n g e r s structures for the calcium loops we have suggested on the basis of NMR evidence that the calcium-sites are floppy and readjust on binding calcium moving helices relative to one another,(see Fig. 1). 5. A more dramatic rearrangement of this protein is required to explain our data.

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