Titlebook: Calcium-Binding Protein Protocols; Volume 1: Reviews an Hans J. Vogel Book 2002 Humana Press 2002 Amino acid.Calcium.chemistry.membrane.pro

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Crystal Structure of Calpain and Insights into Ca2+-Dependent Activationc approx 80-kDa subunit and a common regulatory approx 28-kDa subunit. Although the exact physiological roles of calpains remain to be elucidated, their functional characteristics and wide distribution suggest that they have important cellular roles, which have been reviewed elsewhere (.-.).

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The Multifunctional S100 Protein Family stimulation (..). Their pleiotropic intra- and extracellular functions are consistent with their distinct affinities for Ca., Zn., and Cu., their binding to diverse target proteins, and different post-translational modifications.

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α-Lactalbumin and (Calcium-Binding) Lysozyme decreased by 20-32 degrees. α-Lactalbumin was confirmed by flame spectrophotometry to bind one calcium ion tightly (.). The binding constant for calcium ions to α-lactalbumin has been determined with a variety of methods and the results have been summarized by Kronman (.).

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Neurocalcinestablishes the dark potential of the cell. The decrease in intracellular Ca. that occurs upon illumination stimulates cyclase activity (.). It has only recently been established that a calcium-binding protein called Guanylate cyclase activating protein (GCAP) is responsible for this regulation (.).

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