We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
三色雷蘑核糖核酸酶的分离纯化和理化性质.
- Authors
耿雪冉; 张巧毅; 常明昌; 徐丽婧; 程艳芬; 王贺祥
- Abstract
A ribonuclease (RNase) was purified from Leucopaxillus tricolor fruit bodies by ion exchange chromatography (DEAE-Cellulose,CM-Cellulose and SP-Sepharose) and gel filtration (Superdex 75 HR10/300 GL). The purification fold of this RNase was 154 and the specific activity was 1406 U/mg. Four amino acid sequences were obtained (DMAVSYLSR,IGLSSIPR,ILGRFVVDTYK and SGKANAATPK) by HPLC-LTQ-Orbitrap identification of the RNase. The relative molecular mass of the RNase was estimated to be 15000. The enzyme displayed pH and temperature optima of 9.0 and 40 °C, respectively.The enzyme showed good thermal stability and could remain more than 90% of the activity after 1 h exposure to 80 °C.The enzyme activity was inhibited by Cu2+, Ca2+, Mn2+, Cd2+ and Al3+ at concentration of 1.25~10 mmol/L and the inhibition effect increased with the increase of metal ion concentration. The enzyme activity was stimulated by Fe2+ at concentration of 1.25~5 mmol/L and Pb2+, Zn2+, Mg2+, Hg2+, Fe3+ at concentration of 1.25~2.5 mmol/L.
- Subjects
AMINO acid sequence; ION exchange chromatography; MOLECULAR weights; METAL ions; THERMAL stability; HEAVY metals; CALCIUM ions
- Publication
Acta Edulis Fungi, 2019, Vol 26, Issue 2, p59
- ISSN
1005-9873
- Publication type
Article
- DOI
10.16488/j.cnki.1005-9873.2019.02.009