A highly efficient procedure for purifying the ribosome-inactivating proteins alpha- and beta-momorcharins from Momordica charantia seeds, N-terminal sequence comparison and establishment of their N-glycosidase activity
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摘要A new purification scheme, involving two successive ion exchange chromatographic steps on DEAF-cellulose and Mono-S FPLC, was developed for the isolation of the ribosome-inactivating proteins, alpha- and beta-momorcharins, from the Chinese herb Kuquazi (seeds of Momordica charantia). This simple and rapid procedure yielded 3.1 and 1.7 mg of alpha- and beta-momorcharins, respectively, from 2.5 g of decorticated seeds in only two days. The N-terminal amino acid sequence of beta-momorcharin was found to be DVNFDLSTATAKTYTKFIED. It differed from that of alpha-momorcharin (DVSFRLSGADPRSYGMFIKD) in 10 out of the 20 positions investigated. Like other ribosome-inactivating proteins, the purified momorcharins showed specific N-glycosidase activity at nanomolar concentrations, when rRNA from rabbit reticulocyte lysate was used as substrate. The N-glycosidase activity of both momorcharins was optimal at pH7, not inhibited by K+ and not appreciably affected by NH4+. The activity of alpha-momorcharin was not drastically altered by Mn2+ but (1-10mM) Mn2+ inhibited the activity of beta-momorcharin by about 40%.
著者Fong WP, Poon YT, Wong TM, Mock JWY, Ng TB, Wong RNS, Yao QZ, Yeung HW
期刊名稱Life Sciences
出版年份1996
月份8
日期9
卷號59
期次11
出版社PERGAMON-ELSEVIER SCIENCE LTD
頁次901 - 909
國際標準期刊號0024-3205
電子國際標準期刊號1879-0631
語言英式英語
關鍵詞Momordica charantia; N-glycosidase; purification; ribosome-inactivating proteins; RNA
Web of Science 學科類別Medicine, Research & Experimental; MEDICINE, RESEARCH & EXPERIMENTAL; Pharmacology & Pharmacy; PHARMACOLOGY & PHARMACY; Research & Experimental Medicine

上次更新時間 2020-18-10 於 01:34