Abstract
Natural bovine seminal RNase possesses a potent antitumor action. We have mutagenized monomeric bovine pancreatic RNase A, devoid of any cytotoxic action, to insert residues present at corresponding positions in the subunit of dimeric, antitumor, seminal RNase. Like naturally dimeric seminal RNase, the mutant dimeric RNases display selective toxicity for malignant cells, which is absent in the monomeric mutants.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Substitution*
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Animals
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Antineoplastic Agents / chemistry
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Cattle
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Models, Molecular
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Mutation
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Recombinant Proteins / chemistry
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Ribonuclease, Pancreatic / chemistry*
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Ribonuclease, Pancreatic / genetics
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Ribonuclease, Pancreatic / physiology
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Structure-Activity Relationship
Substances
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Antineoplastic Agents
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Recombinant Proteins
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Ribonuclease, Pancreatic