Related Experiment Video
Updated: Mar 19, 2026

Colorimetric Analysis of Alkaline Phosphatase Activity in S. aureus Biofilm
Published on: April 12, 2019
Isozymes of Bighead Shrimp Alkaline Phosphatase
1a Institute of Botany, Academia Sinica , Nankang, Taipei , Taiwan , R.O.C. and Institute of Marine Biotechnology, National Taiwan Ocean University , Keelung , Taiwan , R.O.C.
Abstract:
Three alkaline phosphatase isozymes, named APase-I, II, and III, were isolated from the cephalothoraxes of bighead shrimp (Solenocera melantho). The molecular weights of APase-I, II, and III estimated by SDS-PAGE were 88.6, 53, and 20 kDa, respectively. They were all glycosylated monomeric enzymes. The optimum pH of APase-I and II were 10 and 8, and the pH ranges for maximum stability were 8.0-12.5 and 5.0-8.0, respectively. Both enzymes showed optimum temperature around 37°C. Arrehnius plots for enzyme thermal inactivation showed that APase II was more stable than APase I above 18°C but less stable below this temperature. Both enzymes showed the highest activities toward aryl phosphate esters among several phosphoesters tested. The Km for p-nitrophenyl phosphate were 0.14 and 4.44 mm for APase I and II, respectively. Na(+) stimulated both enzyme activities in physiological concentration range. APase I was less susceptible to denaturating agents and inhibitors than Apase II.
Related Concept Videos
Cell Specific Gene Expression
Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...

