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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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The Caseins of Milk as Calcium-Binding Proteinsembled into proteins on the ribosomes of the highly developed rough endoplasmic reticulum. All proteins of mammary origin have conserved leader sequences which cause insertion of the nascent proteins into the lumen of the endoplasmic reticulum (..). The proteins are then transported through the Golg
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Skeletal Muscle Troponin C, methodologies have since been developed using molecular biology strategies to express and purify homogeneous preparations of TnC, TnI, and TnT. Other advantages of these recombinant techniques include the ability of producing site-specific mutants and isolated fragments for studying specific regio
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Purification of Recombinant Calbindin D9kesence of ethylenediaminetetracetic acid (EDTA). The third step, gelfiltration, is used to remove small proteins, peptides, and other . components that do not elute from the ion exchange column with any distinct pattern. The fourth step is anion-exchange chromatography in the presence of calcium. Be
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Cadherinsium binding and protein-protein interactions in cadherins (.,.). In this chapter, we will describe a variety of techniques that have been employed to study the function and structure of cadherin molecules. Because there is an excellent review of the protocols for the investigation of cadherin cellul
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Purification and Characterization of ALG-2 A Novel Apoptosis-Linked Ca2+-Binding Proteinns unclear. The uncertainty that existed regarding the absolute nature of Ca.’s relationship to apoptosis was largely caused by the lack of Ca.-dependent molecular targets, which are directly associated with cell death.
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1064-3745 . The primary emphasis is on protein chemistry and biophysical methods. Many of the methods described will also be applicable to proteins that do not bind calcium. Calcium-Binding Protein Proto978-1-61737-135-6978-1-59259-183-1Series ISSN 1064-3745 Series E-ISSN 1940-6029
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