Abstract
There is evidence for the presence of a class of soluble proteins that bind intracellular calcium ions and may be involved in controlling intracellular calcium ion concentrations (1). Among various calcium-binding proteins, spot 35-protein is isolated originally from the soluble fraction of the rat and bovine cerebella and characterized as having a molecular weight of 27,000 daltons and a pI of 5.3. It is localized in the cerebellar Purkinje cells throughout entire neuronal domains including dendritic trees, spines, and axon terminals (2,3). By the molecular cloning and nucleotide sequence of complementary DNA to messenger RNA, Yamakuni et al. (4,5) have revealed a high homology in amino acid sequences (79%) and in the nucleotide sequences (77%) between spot 35-protein and 28k-vitamin D-dependent intestinal calcium-binding protein of chicks (CaBP-28k, chick calbindin), which was identified earlier, and thus its localization has been much more extensively studied than spot 35-protein (6–14).
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Kondo, H., Yamamoto, M., Goto, K. (1990). Immunohistochemical and In Situ Hybridization. Evidence for a Calcium-Binding Protein in the Sinus Nerve. In: Eyzaguirre, C., Fidone, S.J., Fitzgerald, R.S., Lahiri, S., McDonald, D.M. (eds) Arterial Chemoreception. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-3388-6_5
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DOI: https://doi.org/10.1007/978-1-4612-3388-6_5
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