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- W1993060769 abstract "Calreticulin is a 60-kDa Ca2+-binding protein of the endo(sarco)plasmic reticulum membranes of a variety of cellular systems. The protein binds ∼25 mol of Ca2+ with low affinity and ∼1 mol of Ca2+ with high affinity and is believed to be a site for Ca2+ binding/storage in the lumen of the endo(sarco)plasmic reticulum. In the present study, we describe purification procedures for the isolation of recombinant and native calreticulin. Recombinant calreticulin was expressed in Escherichia coli, using the glutathione S-transferase fusion protein system, and was purified to homogeneity on glutathione-Sepharose followed by Mono Q FPLC chromatography. A selective ammonium sulfate precipitation method was developed for the purification of native calreticulin. The protein was purified from ammonium sulfate precipitates by diethylaminoethyl-Sephadex and hydroxylapatite chromatography procedures, which eliminates the need to prepare membrane fractions. The purification procedures reported here for recombinant and native calreticulin yield homogeneous preparations of the proteins, as judged by the HPLC reverse-phase chromatography and by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Purified native and recombinant calreticulin were identified by their NH2-terminal amino acid sequences, by their Ca2+ binding properties, and by their reactivity with anticalreticulin antibodies." @default.
- W1993060769 created "2016-06-24" @default.
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- W1993060769 date "1992-08-01" @default.
- W1993060769 modified "2023-09-28" @default.
- W1993060769 title "Expression and purification of recombinant and native calreticulin" @default.
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- W1993060769 doi "https://doi.org/10.1016/1046-5928(92)90008-k" @default.
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