Results 221 to 230 of about 9,655 (264)
Some of the next articles are maybe not open access.
The 5′-Nucleotidases and Cyclic Phosphodiesterases (3′-Nucleotidases) of the Enterobacteriaceae
Journal of Bacteriology, 1968All members of the Enterobacteriaceae possess distinct 5′-nucleotidases and cyclic phosphodiesterases (3′-nucleotidases) that can be differentiated from the acid and alkaline phosphatases and the acid sugar hydrolases. The nucleotidases and cyclic phosphodiesterases of the various Enterobacteriaceae
openaire +2 more sources
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
openaire +2 more sources
5′-nucleotidase of chicken liver
Biochimica et Biophysica Acta (BBA) - Enzymology, 19671. 1.|5′-Nucleotidase (5′-ribonucleotide phosphophydrolase, EC 3.1.3.5) was partially purified from chicken liver. This is the first time it has been possible to obtain 5′-nucleotidase from the hepatic tissue of uricotelic animals and it was found to be kinetically distinct from 5′-nucleotidases obtained from other sources. 2.
R, Itoh, A, Mitsui, K, Tsushima
openaire +2 more sources
Erythrocyte Pyrimidine 5′‐Nucleotidase
British Journal of Haematology, 1980Summary In this study 31 family members of a patient with erythrocyte pyrimidine 5′‐nucleotidase deficiency were studied. The activity of this enzyme in their erythrocytes is compared with levels in normal subjects and the problems surrounding heterozygote detection are discussed.
J D, Torrance, D, Whittaker, T, Jenkins
openaire +2 more sources
The Histochemical Journal, 1969
Under assay conditions such that there is minimal interference by lysosomal acid phosphatase, the dephosphorylation of nucleoside-5′-monophosphates (AMP or UMP) by rat-liver homogenates at alkaline pH values is attributable to a Mg2+-dependent enzyme (5′-nucleotidase, EC 3.1.3.5).
A A, el-Aaser, E, Reid
openaire +2 more sources
Under assay conditions such that there is minimal interference by lysosomal acid phosphatase, the dephosphorylation of nucleoside-5′-monophosphates (AMP or UMP) by rat-liver homogenates at alkaline pH values is attributable to a Mg2+-dependent enzyme (5′-nucleotidase, EC 3.1.3.5).
A A, el-Aaser, E, Reid
openaire +2 more sources
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 ...
openaire +2 more sources
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.
openaire +2 more sources