PHOSPHORYLASE IN HUMAN SKIN

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Absence of Methylthioadenosine Phosphorylase in Human Gliomas1

All normal mammalian tissues contain methylthioadenosine phosphorylase, which plays a role in the recycling of purines and methionine consumed during polyamine synthesis. A complete deficiency of methyl thioadenosine phosphor) lase has been reported in some human leukemias and lymphomas and in a few solid tumors. The exact incidence of the enzyme deficiency among fresh human tumor specimens has...

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Puke Nucleoside Phosphorylase from Human Erythrocytes

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Purine nucleoside phosphorylase from human erythrocytes.

Purine nucleoside phosphorylase has been purified about 7,300-fold and crystallized from human erythrocytes (mol wt 81,000). The recrystallized enzyme exists in the form of needles and sometimes bundles of needles and has a specific activity of 96 pM units per mg of protein. A number of phenomena reported earlier for a less pure preparation of this enzyme are still seen with the crystalline enz...

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Human deoxycytidine kinase as a deoxyribonucleoside phosphorylase.

Human deoxycytidine kinase (dCK) is a key enzyme in the 5'-phosphorylation of purine and pyrimidine deoxynucleosides with deoxycytidine as the most efficient substrate. The ability of dCK to degrade 2'-deoxyribonucleosides to free nucleobases and 2-deoxy-alpha-d-ribofuranose-1-phosphate was demonstrated by 1H-31P correlation spectroscopy and by isotope enzyme kinetic methods. The reaction depen...

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Deficiency of methylthioadenosine phosphorylase in human leukemic cells in vivo.

Cells from 20 patients with leukemia and 9 with solid tumors were assayed for the enzyme methylthioadenosine phosphorylase, which function in both purine and polyamine metabolism in rapidly dividing cells. As determined by autoradiography of viable cells, and by direct enzymatic analysis, samples from one individual with pre-T-cell acute lymphoblastic leukemia and one with common acute lymphobl...

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ژورنال

عنوان ژورنال: Journal of Histochemistry & Cytochemistry

سال: 1956

ISSN: 0022-1554,1551-5044

DOI: 10.1177/4.3.300