Abstract
A ribosome inactivating protein demonstrating a molecular mass of 21 kDa and a novel N-terminal sequence was isolated from seeds of the hairy melon. The purification procedure involved affinity chromatography on Affi-gel blue gel and ion exchange chromatography on CM-Sepharose and Mono S. The protein designated hispin inhibited translation in the cell-free rabbit reticulocyte lysate system with an IC50 of 165 pM and exhibited N-glycosidase activity. Antifungal activity was also observed.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Antifungal Agents / chemistry
-
Antifungal Agents / isolation & purification*
-
Antifungal Agents / pharmacology
-
Chromatography, Affinity
-
Cucumis / embryology*
-
Electrophoresis, Polyacrylamide Gel
-
Molecular Sequence Data
-
Plant Proteins / chemistry
-
Plant Proteins / isolation & purification*
-
Plant Proteins / pharmacology
-
Ribosomes / drug effects*
-
Seeds / chemistry*
Substances
-
Antifungal Agents
-
Plant Proteins