PubMed · 5978431
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A Dahlqvist. 1966-10-19. [Galactoseuria].. https://pubmed.ncbi.nlm.nih.gov/5978431/
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In galactosemia, galactose-1-phosphate (gal-1-P) is not properly metabolized and accumulates in the fetus and after birth in various tissues when lactose or galactose is ingested. Well-treated galactosemics retain a low level of red cell gal-1-P which increases after breaks of diet. The ester is an indicator of the biogenesis of galactose from glucose and has been considered a pathogenic agent by inhibiting enzymes such as glucose-6-phosphatase, glucose-6-phosphate dehydrogenase, phosphoglucomutase, and glycogen phosphorylase, but the evidence remains presumptive. A futile cycle of galactose phosphorylation and dephosphorylation, and the sequestration of phosphorus in gal-1-P are also suspected to play a role in the pathogenesis of galactosemia.
There is circumstantial evidence that defective galactosylation of complex glycoconjugates exists in tissues from galactosemic patients. Whether this is an etiologic factor in the long-term complications of the disorder is not known. Also not evident is the basis for the impaired galactosylation. The hypothesis that abnormally low cellular uridine diphosphate galactose (UDPgal) content is responsible has not been established. There is a tendency for galactosemic red cell UDPgal to be in the low normal range with a high uridine diphosphate glucose to UDP-gal ratio. This may reflect an inability of red cell UDPgal-4'-epimerase to maintain a normal ratio and consequently higher levels of UDPgal. In the more complex white blood cells and cultured fibroblasts, the UDPgal content and the uridine diphosphate glucose to UDPgal ratio of galactosemics are normal. Therefore, defective galactosylation observed in galactosemic fibroblasts must result from a defect in the transfer of galactose from UDPgal to these moieties.
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.