Purification and characterization of a novel ubiquitin-like antitumour protein with hemagglutinating and deoxyribonuclease activities from the edible mushroom Ramaria botrytis.
作者： Rong Zhou , Ya-Jie Han , Min-Hui Zhang , Ke-Ren Zhang , Tzi Bun Ng
DOI: 10.1186/S13568-017-0346-9
关键词: Peptide sequence 、 Deoxyribonuclease 、 Ultracentrifuge 、 Edible mushroom 、 Annexin 、 Molecular biology 、 Sephadex 、 Ubiquitin 、 Biochemistry 、 Biology 、 Ramaria botrytis
摘要: A novel ubiquitin-like antitumour protein (RBUP) was isolated from fruiting bodies of the edible mushroom Ramaria botrytis. The protein was isolated with a purification protocol involving ion exchange chromatography on DEAE-Sepharose fast flow and gel filtration on Sephadex G-75. SDS-PAGE, Native-PAGE and ultracentrifugation analysis disclosed that RBUP was a monomeric protein with a molecular weight of 18.5 kDa. ESI–MS/MS demonstrated that it shared 69% amino acid sequence similarity with Coprinellus …
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