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1 "Calcium binding protein"
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Purification and Properties of Novel Calcium-binding Proteins from Streptomyces coelicolor
Chang, Ji Hun , Yoon, Soon Sang , Lhee, Sang Moon , Park, I Ha , Jung, Do Young , Park, Yong Sik , Yim, Jeong Bin
J. Microbiol. 1999;37(1):21-26.
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AbstractAbstract
Two novel calcium-binding proteins, named CAB-I and CAB-II, have been isolated from Streptomyces coelicolor. Purification of the calcium-binding proteins involved heat treatment, fractionation with ammonium sulfate, acid treatment, anion exchange and hydrophobic interaction column chromatography, FPLC gel filtration, and preparative isoelectric focusing. A chelex competitive assay and ^45Ca autoradiography verified the calcium-binding ability of the proteins. The major band CAB-II has an apparent molecular weight of 26,000 determined by SDS-polyacrylamide gel electrophoresis and 340,000 determined by gel filtration. The isoelectric point of this molecule showed the acidic nature of the molecule. N-terminal amino acid sequence analysis shows homology to rat Ca^2+/calmodulin-dependent protein kinase-II (CAB-II) and yeast phosphoprotein phosphatase (CAB-I).

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