Comparison of electrophoretic and immunological properties of γ-glutamly transpeptidase from human adult liver, fetal liver and primary hepatoma

Selvaraj, P. ; Balasubramanian, K. A. (1983) Comparison of electrophoretic and immunological properties of γ-glutamly transpeptidase from human adult liver, fetal liver and primary hepatoma Enzyme, 30 (1). pp. 21-28. ISSN 0013-9432

Full text not available from this repository.

Abstract

γ-Glutamyl transpeptidase (γ-GT) from human fetal liver, normal adult liver and primary hepatoma was separated into a hydrophobic form (detergent-solubilized, native enzyme) and a hydrophilic form (papain-digested enzyme) using papain digestion and phenyl Sepharose CL-4B hydrophobic chromatography. On polyacrylamide slab gel electrophoresis the hydrophobic form of the enzyme from the above three sources did not enter the gel, whereas the hydrophilic form entered the gel and moved as a single band with identical mobility. Neuraminidase treatment decreased the mobilities of hydrophilic form of γ-GT from all the three sources to a similar extent suggesting that the enzymes were sialylated equally. The enzyme activities from all the three sources were inhibited and precipitated equally by antibody to fetal liver γ-GT. In Ouchterlony double diffusion test the precipitin lines formed between enzymes from the three sources and anti-fetal liver γ-GT showed a reaction of complete identity. The activity of the hydrophilic form of the enzyme was more inhibited and required less amount of antibody for precipitation compared to their hydrophobic forms of the enzyme from all the three sources.

Item Type:Article
Source:Copyright of this article belongs to International Society for Clinical Enzymology.
ID Code:72192
Deposited On:28 Nov 2011 06:28
Last Modified:28 Nov 2011 06:28

Repository Staff Only: item control page