Some aspects of purine nucleotide metabolism in lymphocytes of B-CLL.
The authors studied the behavior of some enzymes involved in purine nucleotide metabolism in human peripheral blood lymphocytes from normal and B-cell chronic lymphocytic leukemia subjects. Determinations were made with radiochemical methods associated with high performance liquid chromatography. Results indicated a marked increase in de novo purine synthesis enzymes, particularly those of the "inosinic branch point". The latter were absent in normal lymphocytes, whereas they were well evident in leukemic lymphocytes, with the exception of AMP-S synthetase. Whereas the enzymes of the "salvage pathway" were spared in comparison to other proteins, those of the "catabolic pathway" significantly decreased. The authors discuss the possibility that such enzymes may be used as tumor markers.
Tabucchi
A
A
Istituto di Chimica Biologica, Facoltà di Medicina e Chirurgia, Università di Siena Italy.
Leoncini
R
R
Pagani
R
R
Pizzichini
M
M
Terzuoli
L
L
Vannoni
D
D
Porcelli
B
B
Marinello
E
E
Dispensa
E
E
D000659:AMP Deaminase / Q000032:analysis; D000228:Adenine Phosphoribosyltransferase / Q000032:analysis; D000368:Aged; D000369:Aged, 80 and over; D006801:Humans; D007041:Hypoxanthine Phosphoribosyltransferase / Q000032:analysis; D015451:Leukemia, Lymphocytic, Chronic, B-Cell / Q000201:enzymology*; D008875:Middle Aged; D011685:Purine Nucleotides / Q000378:metabolism*
D011685:Purine Nucleotides; D000228:Adenine Phosphoribosyltransferase; D007041:Hypoxanthine Phosphoribosyltransferase; D000659:AMP Deaminase