Kinetic properties of PGM1 and PGM2 phosphoglucomutase "primary" isoenzymes from human erythrocytes were studied. The two enzyme forms share a "ping-pong" kinetic mechanism and show similar Km for substrate (glucose 1-P) and cofactor (glucose 1,6-P2). Micromolar concentrations of fructose 1,6-P2 and glycerate 2,3-P2 inhibit both PGM1 and PGM2 isoenzymes to a similar extent. The sole PGM2 form is affected by ribose monophosphates (ribose 1-P and ribose 5-P) that act as mutase inhibitors vs. glucose 1,6-P2 and as apparent activators vs. glucose 1-P. The interaction between PGM2 isoenzyme and ribose monophosphates is discussed in the light of the ability of this form to also display phosphoribomutase activity.

2,3-Diphosphoglycerate↗

PubMedDate not supplied

[Epigenetic role of magnetic field exposure in tumor progression: fine-tuning experimental models].

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Cell Line, Tumor↗

PubMedDate not supplied

Fast CYP2E1 genotyping using automated fluorescent detection.

BACKGROUND: Among polymorphic genes coding for xenobiotic-metabolizing enzymes, the ethanol-inducible CYP2E1 gene (1667 bp) is known to play a major role in the metabolism ofseveral chemicals. OBJECTIVES: In order to apply large-scale genotyping, we explored the use of a Single Nucleotide Primer Extension (SNuPE) assay coupled with automated fluorescent detection to assess the presence of low-frequency CYP2E1*5B (c2) allele. METHODS: a classic PCR-RFLP (Polymerase Chain Reaction-Restriction Fragment Length Polymorphism) method specific for polymorphic5'-flanking region of CYP2E1 gene was tested in conjunction with a newly developed accelerated SNuPE assay. RESULTS: compared to the classic PCR-RFLP method, the accelerated SNuPE assay proved to be both sensitive and specific for fast CYP2E1 genotyping. CONCLUSIONS: automated fluorescent methods as SNuPE assay are usefulfor public health perspectives, allowing rapid genotyping of metabolic genes in large population studies in clinical or epidemiological settings.

Alleles↗

PubMedDate not supplied

The relevance of glucose 1,6-bisphosphate formation and degradation to human red blood cell metabolism.

In human erythrocytes, in the absence of specific enzymes, G1,6P2 synthesis and degradation are carried out by phosphoglucomutase PGM2 isoenzymes. The results presented, obtained by using partially purified preparations of these enzyme forms, suggest that erythrocyte G1,6P2 may play a crucial role in the physiological interconversion of several important sugar monophosphates.

Erythrocytes↗