Interaction of human intestinal and hepatoma alkaline phosphatases with immobilized Cibacron Blue F3GA.

Abstract

Possible interactions of human liver and intestinal alkaline phosphatases with Cibacron Blue F3GA were examined. The results indicated that the intestinal enzyme bound to the dye column whereas the liver enzyme did not. The affinity of intestinal alkaline phosphatase with the dye-ligand appeared to be biospecific, since a low concentration of purine nucleoside phosphates or potassium phosphate specifically reversed the binding. Taking advantage of the variant alkaline phosphatase from human hepatocellular cancer tissue to behave on the dye adsorbent in a similar fashion with the intestinal enzyme, it was purified by Cibacron Blue F3GA affinity chromatography, producing a 189-fold purification with a yield of 93%.

• Authors: H Yamamoto, M Tanaka, T Okochi, S Kishimoto
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 111 Issue 1 Pg. 36-40 (Feb 28 1983) ISSN: 0006-291X [Print] United States
• PMID: 6830599 (Publication Type: Journal Article)

Chemical References

• Triazines
• Cibacron Blue F 3GA
• Alkaline Phosphatase

Topics

• Alkaline Phosphatase (isolation & purification, metabolism)
• Chromatography, Affinity
• Humans
• Intestine, Small (enzymology)
• Liver (enzymology)
• Liver Neoplasms (enzymology)
• Triazines (metabolism)