Identification, separation and characterisation of two forms of cytosolic 5'-nucleotidase/nucleoside phosphotransferase in calf thymus. 1998

R Pesi, and C Baiocchi, and S Allegrini, and E Moretti, and F Sgarrella, and M Camici, and M G Tozzi
Dipartimento di Fisiologia e Biochimica, Università di Pisa, Italy.

Cytosolic 5'-nucleotidase, acting preferentially on IMP, GMP and their deoxyderivatives, endowed with phosphotransferase activity, is a widespread enzyme responsible for the regulation of intracellular IMP and GMP concentrations and the phosphorylation of purine nucleoside pro-drugs. The enzyme activity is stimulated by ATP, ADP and 2,3-bisphosphoglycerate (BPG), and is inhibited by phosphate. Calf thymus possesses two active proteins with a different electrophoretic mobility. In this report we show that the two forms can be separated by ADP-agarose affinity chromatography. Whereas form A binds weakly to the column, form B is tightly bound and is released by the addition of ADP into the elution buffer. The two enzyme forms differ in terms of electrophoretic, chromatographic behaviour and regulatory characteristics. Form B, as already described for the enzyme purified from the same source (Pesi et al., 1996, Biochim Biophys Acta 294, 191-194), exhibits three different sites for the three activators with a synergistic effect between ADP and BPG. Form A has a high affinity regulatory site for BPG, while ADP and ATP appear to share the same low affinity site and no synergistic effect is observed.

UI MeSH Term Description Entries
D010770 Phosphotransferases A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7. Kinases,Phosphotransferase,Phosphotransferases, ATP,Transphosphorylase,Transphosphorylases,Kinase,ATP Phosphotransferases
D002417 Cattle Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor. Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
D002846 Chromatography, Affinity A chromatographic technique that utilizes the ability of biological molecules, often ANTIBODIES, to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Chromatography, Bioaffinity,Immunochromatography,Affinity Chromatography,Bioaffinity Chromatography
D000244 Adenosine Diphosphate Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position. ADP,Adenosine Pyrophosphate,Magnesium ADP,MgADP,Adenosine 5'-Pyrophosphate,5'-Pyrophosphate, Adenosine,ADP, Magnesium,Adenosine 5' Pyrophosphate,Diphosphate, Adenosine,Pyrophosphate, Adenosine
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013950 Thymus Gland A single, unpaired primary lymphoid organ situated in the MEDIASTINUM, extending superiorly into the neck to the lower edge of the THYROID GLAND and inferiorly to the fourth costal cartilage. It is necessary for normal development of immunologic function early in life. By puberty, it begins to involute and much of the tissue is replaced by fat. Thymus,Gland, Thymus,Glands, Thymus,Thymus Glands
D015151 Immunoblotting Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies. Dot Immunoblotting,Electroimmunoblotting,Immunoelectroblotting,Reverse Immunoblotting,Immunoblotting, Dot,Immunoblotting, Reverse,Dot Immunoblottings,Electroimmunoblottings,Immunoblottings,Immunoblottings, Dot,Immunoblottings, Reverse,Immunoelectroblottings,Reverse Immunoblottings
D015720 5'-Nucleotidase A glycoprotein enzyme present in various organs and in many cells. The enzyme catalyzes the hydrolysis of a 5'-ribonucleotide to a ribonucleoside and orthophosphate in the presence of water. It is cation-dependent and exists in a membrane-bound and soluble form. EC 3.1.3.5. 5'-AMP Nucleotidase,AMP Phosphatase,Adenylate Phosphatase,Antigens, CD73,CD73 Antigens,Cytidylate Phosphatase,Ecto-5'-Nucleotidase,IMP Nucleotidase,IMP Phosphatase,Inosinate Phosphatase,Pyrimidine 5'-Nucleotidase,Thymidine Phosphatase,Uridylate 5'-Nucleotidase,5'-Nucleotidase Phosphoribolase,Antigen, CD73,IMPase,5' AMP Nucleotidase,5' Nucleotidase,5' Nucleotidase Phosphoribolase,CD73 Antigen,Ecto 5' Nucleotidase,Pyrimidine 5' Nucleotidase,Uridylate 5' Nucleotidase

Related Publications

R Pesi, and C Baiocchi, and S Allegrini, and E Moretti, and F Sgarrella, and M Camici, and M G Tozzi
February 1994, Journal of biochemical toxicology,
R Pesi, and C Baiocchi, and S Allegrini, and E Moretti, and F Sgarrella, and M Camici, and M G Tozzi
December 1991, Archives of biochemistry and biophysics,
R Pesi, and C Baiocchi, and S Allegrini, and E Moretti, and F Sgarrella, and M Camici, and M G Tozzi
December 1993, Journal of biochemical and biophysical methods,
R Pesi, and C Baiocchi, and S Allegrini, and E Moretti, and F Sgarrella, and M Camici, and M G Tozzi
January 1991, Advances in experimental medicine and biology,
R Pesi, and C Baiocchi, and S Allegrini, and E Moretti, and F Sgarrella, and M Camici, and M G Tozzi
July 1994, Archives of biochemistry and biophysics,
R Pesi, and C Baiocchi, and S Allegrini, and E Moretti, and F Sgarrella, and M Camici, and M G Tozzi
April 1991, Clinical biochemistry,
R Pesi, and C Baiocchi, and S Allegrini, and E Moretti, and F Sgarrella, and M Camici, and M G Tozzi
March 2001, The Journal of biological chemistry,
R Pesi, and C Baiocchi, and S Allegrini, and E Moretti, and F Sgarrella, and M Camici, and M G Tozzi
June 1998, Biochemistry,
R Pesi, and C Baiocchi, and S Allegrini, and E Moretti, and F Sgarrella, and M Camici, and M G Tozzi
January 1980, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
R Pesi, and C Baiocchi, and S Allegrini, and E Moretti, and F Sgarrella, and M Camici, and M G Tozzi
July 1956, Biochimica et biophysica acta,
Copied contents to your clipboard!