Isolation and Characterization of a Type 1 Ribosome-Inactivating Protein from Fruiting Bodies of the Edible Mushroom (Volvariella volvacea).
A novel single-chained ribosome-inactivating protein (RIP) with a molecular weight of approximately 29 000 was purified from fruiting bodies of the edible mushroom Volvariellavolvacea with a procedure involving ammonium sulfate precipitation, ion-exchange chromatography on DEAE-cellulose, and gel filtration on Superdex 75. The mushroom RIP, designated volvarin, exhibited a potent inhibitory action on protein synthesis in the rabbit reticulocyte lysate system with an IC(50) value of 0.5 nM. Like most plant RIPs, volvarin acted as an N-glycosidase that depurinated rRNA from rabbit reticulocyte lysate, releasing a characteristic RNA fragment after treatment with aniline. It also exerted a deoxyribonuclease activity on supercoiled SV-40 DNA and demonstrated a strong abortifacient effect in mice.
Yao
QZ
Department of Biology, Graduate School, Academia Sinica, Beijing, China, and Departments of Biology and Biochemistry, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong.
Yu
MM
Ooi
LS
Ng
TB
Chang
ST
Sun
SS
Ooi
VE