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PMID: 7646508 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Full antitumor action of recombinant seminal ribonuclease depends on the removal of its N-terminal methionine.

Biochemical and biophysical research communications ·Vol. 213 ·No. 2 ·1995-08-15 ·Pages 525-32

Adinolfi BS, Cafaro V, D'Alessio G, Di Donato A

Abstract

Bovine seminal RNase (BS-RNase) is a dimeric member of the pancreatic-like ribonuclease superfamily, with antitumor activity. We report here that recombinant Met(-1) BS-RNase is a less potent cytotoxic factor, while structurally and catalytically indistinguishable from BS-RNase isolated from natural sources. Mature recombinant BS-RNase instead displays full antitumor action. This suggests that the conformation of the N-terminal region of BS-RNase is among the structural determinants of its antitumor action, in addition to its catalytic activity and its quaternary structure.

MeSH Terms

Amino Acid Sequence Animals Antineoplastic Agents/pharmacology Base Sequence Cattle Cell Survival/drug effects Hydrogen-Ion Concentration Macromolecular Substances Male Methionine/chemistry Mice Molecular Sequence Data Mutagenesis, Site-Directed Polymerase Chain Reaction Protein Conformation Recombinant Proteins/chemistry,pharmacology Ribonucleases/chemistry,genetics,pharmacology Seminal Vesicles/enzymology Structure-Activity Relationship Tumor Cells, Cultured

Chemicals

Antineoplastic Agents Macromolecular Substances Recombinant Proteins Methionine Ribonucleases

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Adinolfi B S

Dipartimento di Chimica Organica e Biologica, Università di Napoli Federico II, Italy.

Cafaro V

D'Alessio G

Di Donato A

Article Info

Journal

Biochemical and biophysical research communications

Abbr.

Biochem Biophys Res Commun

ISSN

0006-291X

DOI

10.1006/bbrc.1995.2163

Published

1995-08-15

Pages

525-32

Language

English

Region

United States

NLM ID

0372516

Subset

External Links

PubMed source DOI: 10.1006/bbrc.1995.2163 View journal details

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Full antitumor action of recombinant seminal ribonuclease depends on the removal of its N-terminal methionine.

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