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Micrococcus radiodurans 5′-nucleotidase
Biochimica et Biophysica Acta (BBA) - Enzymology, 1973Abstract A 5′-nucleotidase (5′-ribonucleotide phosphohydrolase, EC 3.1.3.5) isolated from Micrococcus radiodurans appears to have properties more closely resembling some of the corresponding vertebrate enzymes than the reported bacterial enzymes. The M. radiodurans enzyme is a strict nucleoside 5′-phosphomonoesterase with a pH optimum between 8 and 9.
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Diphosphopyridine Nucleotidase and Acute Glomerulonephritis
Archives of Internal Medicine, 1962The presence of diphosphopyridine nucleotidase (DPNase) in filtrates of cultures of hemolytic streptococci was first described in 1956. 1,2 Among several bacterial species studied, only streptococci of Groups A, C, and G produced this extracellular enzyme.
A J, GONZAGA, C H, RAMMELKAMP
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1977
The 5′-mononucleotides are dephosphorylated by the enzyme, 5′-ribonucleotide phosphohydrolase (EC 3.1.3.5), commonly known as 5′-nucleotidase (5′N). This enzyme was first described by Reis (1937, 1939) in heart and skeletal muscle and its specificity established histochemically for 5′-nucleotides by Gomori (1949a,b).
Maryrose Conklyn, Robert Silber
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The 5′-mononucleotides are dephosphorylated by the enzyme, 5′-ribonucleotide phosphohydrolase (EC 3.1.3.5), commonly known as 5′-nucleotidase (5′N). This enzyme was first described by Reis (1937, 1939) in heart and skeletal muscle and its specificity established histochemically for 5′-nucleotides by Gomori (1949a,b).
Maryrose Conklyn, Robert Silber
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5-Nucleotidase activity in lymphocytes
The Histochemical Journal, 1981Some characteristics of lymphocyte 5'-nucleotidase are reviewed. The optimal conditions for the cytochemical localization of 5'-nucleotidase (AMPase) in the mouse lymphocyte have been established. Quantitative monitoring of the effects of fixation and the components of the cytochemical medium showed that cytochemistry can be performed under conditions ...
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