Glucose 1,6-bisphosphate decline in human erythrocytes: possible involvement of phosphoglucomutase PGM2 isoenzymes.
Human erythrocytes incubated with various sugars lower their glucose 1,6-bisphosphate (Glc-1,6-P2) content, as do haemolysates containing exogenous Glc-1,6-P2 incubated with sugar monophosphates (sugar-P). Experiments performed with isolated erythrocyte phosphoglucomutase (PGM) isoenzymes indicate that only definite isoenzymatic forms, namely PGM2, are able to consume Glc-1,6-P2 during the mutation of sugar-P other than glucose-P. In this process a phosphate group is released from Glc-1,6-P2 and can be partially recovered in the biphosphate of the mutated sugar-P. The relevance of this mechanism of Glc-1,6-P2 degradation is discussed in regard to the physiological turnover of the biphosphate.
Ninfali
P
P
Piatti
E
E
Accorsi
A
A
Palma
F
F
Fazi
A
A
Tozzi
M G
MG
Fornaini
G
G
D000227:Adenine Nucleotides / Q000097:blood; D004912:Erythrocytes / Q000378:metabolism*; D019298:Glucose-6-Phosphate / Q000031:analogs & derivatives*; D005958:Glucosephosphates / Q000097:blood*; D006801:Humans; D007527:Isoenzymes / Q000097:blood; D010733:Phosphoglucomutase / Q000097:blood; D012267:Ribosemonophosphates / Q000097:blood; D013403:Sugar Phosphates / Q000097:blood
D000227:Adenine Nucleotides; D005958:Glucosephosphates; D007527:Isoenzymes; D012267:Ribosemonophosphates; D013403:Sugar Phosphates; D019298:Glucose-6-Phosphate; C016473:glucose-1,6-bisphosphate; D010733:Phosphoglucomutase