The Purification of Alkaline Phosphatase
fromEisenia Foetide Sarigng

LI Sui-yan; LI Qing-yi

Volume 15 Issue 5

Oct. 2002

Turn off MathJax

Article Contents

Journal of Southwest Jiaotong University > 2002 > 15(5): 597-600.

LI Sui-yan, LI Qing-yi. The Purification of Alkaline PhosphatasefromEisenia Foetide Sarigng[J]. Journal of Southwest Jiaotong University, 2002, 15(5): 597-600.

Citation:

LI Sui-yan, LI Qing-yi. The Purification of Alkaline Phosphatase fromEisenia Foetide Sarigng[J]. Journal of Southwest Jiaotong University, 2002, 15(5): 597-600.

LI Sui-yan, LI Qing-yi. The Purification of Alkaline PhosphatasefromEisenia Foetide Sarigng[J]. Journal of Southwest Jiaotong University, 2002, 15(5): 597-600.

Citation:

LI Sui-yan, LI Qing-yi. The Purification of Alkaline Phosphatase fromEisenia Foetide Sarigng[J]. Journal of Southwest Jiaotong University, 2002, 15(5): 597-600.

PDF( 0 KB)

The Purification of Alkaline Phosphatase fromEisenia Foetide Sarigng

Publish Date: 25 Oct 2002

Abstract

Abstract

Alkaline phosphatase (AKP) was purified from the cell extracts ofEisenia Foetida Sarigngusing the routine means: n-bulanol extraction, ammonium sulfate fractional precipitation, DEAE-cellulose chromatography, Sephadex G-100 and Sephadex G-200 gel filtration. The purified AKP was found to be homogeneous by polyacrylamide gel disc electrophoresis. Its specific activity is 40.64 units per milligram of protein, and purification multiple is 57.24-fold.
- alkaline phosphatase,
- purification,
- Eisenia Foetide Sarigng