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Purification and characterization of Ulva pertusa Kjellm alkaline phosphatase.

Authors :
Yang D
Wang J
Bao Y
An L
Source :
Preparative biochemistry & biotechnology [Prep Biochem Biotechnol] 2003 May; Vol. 33 (2), pp. 113-23.
Publication Year :
2003

Abstract

The activity of alkaline phosphatase (ALP, EC 3.1.3.1.) was found in seaweeds, including five kinds of green alga, eighteen kinds of red alga, and six kinds of brown alga, collected from the seaside of Dalian in China. The enzyme was purified 1230-fold from Ulva pertusa Kjellm. It had a specific activity of 48.6 U/mg protein and was proven to be homogeneous by SDS-PAGE with a subunit molecular mass of 19.5 kDa. The activity of ALP peaked at pH9.8, and was completely inhibited by DTT and partly by NBS. The Michaelis-Menten constant Km and the maximum reaction velocity Vmax, at pH 9.8 and 37 degrees C were 0.950 mM and 5.00 microM/min, respectively.

Details

Language :
English
ISSN :
1082-6068
Volume :
33
Issue :
2
Database :
MEDLINE
Journal :
Preparative biochemistry & biotechnology
Publication Type :
Academic Journal
Accession number :
12784882
Full Text :
https://doi.org/10.1081/PB-120021436