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Primary structure of β‐momorcharin, a ribosome‐inactivating protein from the seeds of Momordica Charantia Linn (Cucurbitaceae)
Author(s) -
GuoJie Ye,,
BaoYuan Lu,,
ShanWei Jin,,
RuiQing Qian,,
Yu Wang,
Publication year - 1999
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.19990170614
Subject(s) - momordica , cucurbitaceae , chemistry , ribosome inactivating protein , botany , ribosome , traditional medicine , biochemistry , rna , medicine , gene , biology
The complete amino acid sequence of β‐momorcharin, a ribosome‐inactivating protein from the seeds of Momordica charantia Linn (Cucurbitaceae) has been determined. This has been done by the sequence analysis of peptides obtained by enzymatic digestion with trypsin, chymotrypsin and S. aureus V8 protease, as well as by chemical cleavage with BNPS‐skatole. The protein consists of 249 amino acid residues containing one asparagine ‐ linked sugar group attached to the site of Asn 51 and has a calculated relative molecular mass of 28,452 Da without addition of the carbohydrate. Comparison of this sequence with those of trichosanthin and other ribosome‐inactivating proteins from different species of plants shows a significant homology with each other. Regarding the similarity of their biological properties, an active domain of these proteins has been predicted here.