https://scholars.lib.ntu.edu.tw/handle/123456789/452463
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.author | LU-PING CHOW | en_US |
dc.contributor.author | Kamo M. | en_US |
dc.contributor.author | Lin J.-Y. | en_US |
dc.contributor.author | Wang S.-H. | en_US |
dc.contributor.author | Ueno Y. | en_US |
dc.contributor.author | Tsugita A. | en_US |
dc.creator | Lu-Ping Chow;Kamo M.;Lin J.-Y.;Wang S.-H.;Ueno Y.;Tsugita A. | - |
dc.date.accessioned | 2020-01-22T04:48:06Z | - |
dc.date.available | 2020-01-22T04:48:06Z | - |
dc.date.issued | 1996 | - |
dc.identifier.issn | 10217770 | - |
dc.identifier.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029778772&partnerID=40&md5=5deaf6de89ba32648854a9ff580aea90 | - |
dc.identifier.uri | https://scholars.lib.ntu.edu.tw/handle/123456789/452463 | - |
dc.description.abstract | In this study, we sequenced a new type I ribosome-inactivating protein, trichoanguina, from the seeds of Trichosanthes anguina (snake gourd). Trichoanguina is a basic glycoprotein having an apparent molecular mass of 35.0 kD and possessing strong ribosome-inactivating activity. Trichoanguina was cleaved with cyanogen bromide and partially digested with thermolysin, chymotrypsin, trypsin and Staphylococcus aureus V8 protease. The subsequent peptide fragments were separated by SDS-polyacrylamide gel electrophoresis, followed by electroblotting to polyvinylidene difluoride membranes and then sequencing. The sequencing of trichoanguina was completed, consisting of 245 amino acid residues. The sequencing of trichoanguina revealed a considerable homology to trichosanthin and α-trichosanthin, which are known as abortifacient, ribosome-inactivating and antihuman immunodeficiency virus proteins, with 46.7% and 55.6% amino acid identities, respectively. The sequence conserves two active sites: Glu- 158 and Arg- 161. | - |
dc.relation.ispartof | Journal of Biomedical Science | - |
dc.subject | Protein sequence; Ribosome-inactivating protein(s); Trichoanguina; Trichosanthes anguina | - |
dc.subject.classification | [SDGs]SDG3 | - |
dc.subject.other | abortive agent; anti human immunodeficiency virus agent; chymotrypsin; cyanogen bromide; glycoprotein; ribosome inactivating protein; thermolysin; trichoanguina; Trichosanthes extract; trichosanthin; trypsin; unclassified drug; amino acid sequence; article; nonhuman; plant seed; priority journal; protein degradation; sequence homology; Anguina; Cucurbita; Human immunodeficiency virus; Serpentes; Staphylococcus aureus; Trichosanthes; Trichosanthes cucumerina var. anguina | - |
dc.title | Amino acid sequence of trichoanguina, a ribosomal-inactivating protein from Trichosanthes anguina seeds | en_US |
dc.type | journal article | en |
dc.identifier.scopus | 2-s2.0-0029778772 | - |
dc.relation.pages | 178-186 | - |
dc.relation.journalvolume | 3 | - |
dc.relation.journalissue | 3 | - |
item.openairecristype | http://purl.org/coar/resource_type/c_6501 | - |
item.openairetype | journal article | - |
item.grantfulltext | none | - |
item.cerifentitytype | Publications | - |
item.fulltext | no fulltext | - |
crisitem.author.dept | Biochemistry and Molecular Biology | - |
crisitem.author.orcid | 0000-0002-4420-211X | - |
crisitem.author.parentorg | College of Medicine | - |
顯示於: | 生物化學暨分子生物學科研究所 |
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