Abstract
This chapter provides an overview of the seminal ribonuclease. Bovine seminal RNase (BS-RNase) is a diverse RNase “different” from the historic prototype RNase A—and from all other RNases of the vertebrate superfamily—for its dimeric structure, for its non-Michaelian kinetics, and for its special, noncatalytic, biological actions. BS-RNase is also a diverse RNase because it exists in a multiplicity of structural forms, and is endowed with a multiplicity of biological actions. Two quaternary conformations and three isoenzymatic subunit compositions are known for BS-RNase. BS-RNase performs a surprising array of biological actions: aspermatogenic, antitumor, immunosuppressive, and antiviral. BS-RNase may not be the only seminal RNase: an RNase has been purified from human semen and low levels of RNase activity have been detected in the semen of several mammals, including mouse, rabbit, and sheep. This chapter discusses isolation and production of seminal RNase. It explains preparation of seminal ribonuclease from natural sources. Production of recombinant BS-RNase is discussed. The chapter elaborates covalent structure, three-dimensional structure, and folding pathway of seminal RNase. The chapter also outlines the functions of seminal ribonuclease.
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