Shyu Y T, Foegeding P M
Department of Food Science, North Carolina State University, Raleigh 27695-7624.
J Gen Microbiol. 1991 Jul;137(7):1619-23. doi: 10.1099/00221287-137-7-1619.
A novel calcium-binding protein has been purified from the dormant spores of Bacillus cereus T. Purity of this protein was verified by SDS-PAGE and reversed-phase HPLC. Its calcium-binding ability was verified by a competitive calcium-binding assay using Chelex-100 resin and 45Ca autoradiography. The protein is heat-stable and is retained by hydrophobic matrices (phenyl-Sepharose) in a calcium-dependent manner. SDS-PAGE and amino acid composition indicate the molecular mass of the protein to be 24 kDa.
一种新型钙结合蛋白已从蜡样芽孢杆菌T的休眠孢子中纯化出来。通过SDS-PAGE和反相HPLC验证了该蛋白的纯度。利用Chelex-100树脂和45Ca放射自显影技术，通过竞争性钙结合试验验证了其钙结合能力。该蛋白具有热稳定性，并以钙依赖的方式被疏水基质（苯基琼脂糖）保留。SDS-PAGE和氨基酸组成表明该蛋白的分子量为24 kDa。
