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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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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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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 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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5'-Nucleotidase from rat heart
Biochemistry, 19815'-Nucleotidase has been extracted from rat heart and purified to apparent homogeneity. The enzyme is a glycoprotein. Gel electrophoresis in the presence of sodium dodecyl sulfate indicates that the apparent molecular weight of the subunit is 74 000 at several different gel concentrations.
Y, Naito, J M, Lowenstein
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5′-Nucleotidase from bull seminal plasma
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 19835'-Nucleotidase (5'-ribonucleotide phosphohydrolase, EC 3.1.3.5) occurs in bull seminal plasma in multiple forms. The heterogeneity does not reflect the existence of true isoenzymes, but is due to the association of the enzyme with particulate material and to molecular aggregation phenomena. Addition of detergents to native bull seminal plasma prevents
FINI, Carlo +3 more
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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 I from rabbit heart
Biochemistry, 19915'-Nucleotidase I (N-I) from rabbit heart was purified to homogeneity. After ammonium sulfate precipitation, the purification involved chromatography on phosphocellulose, DEAE-Sepharose, AMP-agarose, and ADP-agarose. The pure enzyme has a specific activity of 318 mumol (mg of protein)-1 min-1.
Y, Yamazaki +2 more
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