›› 2011, Vol. 38 ›› Issue (5): 54-57.

• 生理生化 • Previous Articles     Next Articles

Purification of Myeloperoxidase from White Blood Cells of Dairy Cow

SHI Jing, LV Ying, YANG Yu, LI Qing-zhang   

  1. Key Laboratory of Dairy Science,Ministry of Education,Northeast Agricultural University,Harbin 150030,China
  • Received:2010-10-15 Revised:1900-01-01 Online:2011-05-20 Published:2011-05-20

Abstract: The protein myeloperoxidase(MPO) was isolated and purified from bovine whole blood by Sephadex G-200 chromatography and ConA-Sephrose 4B affinity chromatography. The activity,molecular weight,rate of purity and protein concentration of MPO were 0.068 U/mL,64.7,47.9,13.4 ku,94.2% and 147.3 μg/mL,respectively. The method developed for the isolation and purification of MPO was important for the following research.

Key words: dairy cow; myeloperoxidase; purification

CLC Number: