Isolation and Purification of Protein from Ovis aries Placenta
摘要
The total protein extract of sheep placenta was fractionated by tandem anion-exchange chromatography over Toyopearl DEAE-650M and gel filtration over Toyopearl HW-55F. The obtained homogeneous protein exhibited antiproliferative activity in HeLa and HCT-116 cell culture (IC50 0.80 ± 0.27 and 1.73 ± 0.03 mg/mL, respectively). The amino-acid composition of the purified protein was determined. Tandem mass spectral sequencing and subsequent annotation using a database identified the purified protein as a calponin homolog.