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Catalytic Activity of Bovine Seminal Ribonuclease is Essential for Its Immunosuppressive and Other Biological Activities

Overview
Journal Biochem J
Specialty Biochemistry
Date 1995 Jun 1
PMID 7772040
Citations 26
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Abstract

Bovine seminal ribonuclease (BS-RNase) is a homologue of RNase A with special biological properties, including potent immunosuppressive activity. A mutant BS-RNase was created in which His-119, the active-site residue that acts as a general acid during catalysis, was changed to an aspartic acid. H119D BS-RNase formed a dimer with quaternary structure similar to that of the wild-type enzyme but with values of kcat. and kcat./Km for the cleavage of UpA [uridylyl(3'-->5')adenosine] that were 4 x 10(3)-fold lower. The mutant protein also demonstrated dramatically decreased immunosuppressive, anti-tumour, aspermatogenic, and embryotoxic activities. The catalytic activity of BS-RNase is therefore necessary for its special biological properties.

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References
1.
DAlessio G, Floridi A, De Prisco R, Pignero A, Leone E . [Bull semen ribonucleases. 1. Purification and physico-chemical properties of the major component]. Eur J Biochem. 1972; 26(2):153-61. DOI: 10.1111/j.1432-1033.1972.tb01751.x. View

2.
Soucek J, CHUDOMEL V, Potmesilova I, Novak J . Effect of ribonucleases on cell-mediated lympholysis reaction and on GM-CFC colonies in bone marrow culture. Nat Immun Cell Growth Regul. 1986; 5(5):250-8. View

3.
Youle R, Newton D, Wu Y, Gadina M, Rybak S . Cytotoxic ribonucleases and chimeras in cancer therapy. Crit Rev Ther Drug Carrier Syst. 1993; 10(1):1-28. View

4.
Cleland W . Statistical analysis of enzyme kinetic data. Methods Enzymol. 1979; 63:103-38. DOI: 10.1016/0076-6879(79)63008-2. View

5.
Ipata P, FELICIOLI R . A spectrophotometric assay for ribonuclease activity using cytidylyl-(3',5')-adenosine and uridylyl-(3',5')-adenosine as substrates. FEBS Lett. 1968; 1(1):29-31. DOI: 10.1016/0014-5793(68)80010-9. View