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Purification and characterization of cytoplasmic 5′(3′)-nucleotidase from rabbit spleen: characteristic differences of the enzyme from the rat spleen nucleotidase

Authors
Journal
Comparative Biochemistry and Physiology Part B Comparative Biochemistry
0305-0491
Publisher
Elsevier
Publication Date
Volume
103
Issue
2
Identifiers
DOI: 10.1016/0305-0491(92)90311-e
Disciplines
  • Biology
  • Chemistry

Abstract

Abstract 1. 1. A 5′(3′)-nucleotidase, which preferably hydrolyzed 3′-dTMP and 3′-dUMP, was highly purified from rabbit spleen cytosol. 2. 2. The enzyme also hydrolyzes 3′-UMP, 5′-dUMP and guanine nucleotides, but does not hydrolyze any adenine nucleotides or cytosine nucleotides. 3. 3. The activity is dependent upon Mg 2+, Co 2+ or Mn 2+; the addition of deoxyinosine stimulates the activity, and the pH optimum for the hydrolysis of 3′-dTMP is 7.0. 4. 4. Although the catalytic properties of the enzyme are similar to the 5′(3′)-nucleotidase from rat spleen, these nucleotidases differ in their molecular disposition. 5. 5. The charge state of the rabbit enzyme is slightly basic, and the subunit r is about 27kDa, while the value of the rat enzyme is 26 kDa. 6. 6. Immunochemical experiments with the use of antibodies against the purified nucleotidase indicate that enzymes from rabbit spleen and from rat spleen are composed of different polypeptides.

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