Isolation and Purification of Protein from Ovis aries Placenta.

Autor: Hu, A. L., Wali, A., Zhao, X. M., Turdu, G., Gao, Y. H., Yang, Z., Kelaimu, R., Mavlonov, G. T., Mamadrakhimov, A. A., Aisa, H. A., Yili, A.
Předmět:
Zdroj: Chemistry of Natural Compounds; Nov2024, Vol. 60 Issue 6, p1119-1122, 4p
Abstrakt: 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. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index