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Clinical Biochemistry, 1970
Summary 1. Sequential studies of serum 5′-nucleotidase (EC 3.1.3.5) in association with other enzymes in patients with malignant diseases are presented. 2. Evidence is given for the specific significance of the assay of 5′-nucleotidase in serum which is a sensitive monitor for the appearance of metastases in liver. 3.
W, van der Slik +3 more
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Summary 1. Sequential studies of serum 5′-nucleotidase (EC 3.1.3.5) in association with other enzymes in patients with malignant diseases are presented. 2. Evidence is given for the specific significance of the assay of 5′-nucleotidase in serum which is a sensitive monitor for the appearance of metastases in liver. 3.
W, van der Slik +3 more
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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
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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
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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
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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
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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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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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5′-Nucleotidase and phosphatases in human brain
Clinica Chimica Acta, 1964Abstract The activities of five enzymes catalysing release of phosphate have been determined in homogenates from different regions of human brain and cord; all enzymes showed activities within a small range of absolute values. The enzymes showed similar activities in autopsy and biopsy material.
N, ROBINSON, B M, PHILLIPS
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5′-Nucleotidase Activities in Human Fetus
Biology of the Neonate, 2009Specific 5′-nucleotidase (5′-N) activity in 17 human fetuses was systemically studied in order to get basic values of the enzyme activity. A wide spectrum of 5′-N activity among the organs was revealed. Very strong activity was found in placenta (42.62 ± 19.24 nmol adenosine/mg protein/min), skeletal muscle (31.80 ± 11.10) and skin (27.31 ± 13.00 ...
S, Amano +5 more
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