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Catalytic activity of bovine seminal ribonuclease is essential for its immunosuppressive and other biological activities
Cited 70 time in
Web of Science
Cited 69 time in Scopus
- Authors
- Issue Date
- 1995-06
- Publisher
- Portland Press, Ltd.
- Citation
- Biochemical Journal, Vol.308, pp.547-550
- 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 k(cat) and k(cat.)/K-m for the cleavage of UpA [uridylyl(3' --> 5')adenosine] that were 4x10(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.
- ISSN
- 0264-6021
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