PubMed · 5529786
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S Nakamura, K Tokita, K Kera, K Sasaki. 1970. [Galactose loading test].. https://pubmed.ncbi.nlm.nih.gov/5529786/
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The D-galactose-binding lectin (PA-I) from the bacterium Pseudomonas aeruginosa, isolated by affinity chromatography on Sepharose, was examined for its relative affinities for simple sugars and their derivatives using equilibrium dialysis and hemagglutination inhibition tests. The lectin, which was found to bind 0.68 mol of D-galactose per subunit of 12.8 kDa, exhibited an association constant (Ka) of 3.4 x 10(4) M-1 for D-galactose and higher affinities for hydrophobic and thio derivatives of D-galactose (with highest affinity for the hydrophobic thio derivatives). alpha-Methyl-galactoside was a stronger inhibitor than the beta-methyl derivative and alpha-lactose was a weak inhibitor but the hydrophobic phenylated derivatives of the beta-configuration of D-galactose were more potent inhibitors than the respective alpha-galactosides.
The authors discuss a simple method for assessment of the galactose elimination capacity after intravenous administration of a 20% solution, total dose 0.5 g galactose/kg body weight. In six blood venous samples after termination of an infusion (after 25, 30, 35, 40, 45 and 50 minutes) from an inserted venous catheter after assessment of the enzymatic estimation of the galactose concentration in individual samples the elimination line of galactose is assessed as well as its point of intersection (t) with the time axis. By means of these data along with the data on the amount of injected galactose and the amount of galactose excreted in the urine the galactose elimination capacity is calculated. The method is suitable for evaluation and monitoring of the functional state of the liver. It reflects the functional mass of liver parenchyma and is therefore a quantitative test of liver function.
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