Search

Copyright of Journal of Liaoning Technical University (Natural Science Edition) / Liaoning Gongcheng Jishu Daxue Xuebao (Ziran Kexue Ban) is the property of Journal of Liaoning Technical University (Natural Science) Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Guihaia is the property of Guihaia Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Volatile terpenes are important aroma active compounds in flowers and fruits of plant. Diversities of terpenes are usually determined by type and function of terpene synthase in different species. Osmanthus fragrans is an important fragrant plant, in which terpenes are the important components of floral scent. But there are few studies on terpene synthase in O. fragrans. To reveal the biosynthesis mechanism of terpenes in O. fragrans, we predicted the physicochemical properties, subcellular localization and structure of four TPS proteins by bioinformatics, and expressed them in prokaryotic expression system. Finally, the function of soluble TPS4 recombinant protein was analyzed by enzyme reaction in vitro. The results were as follows:(1)The physicochemical properties of the four TPS proteins had relatively little difference. Only TPS4 protein locating in other targets without signal peptide had low proportional extended strand and no extended strand near amidogen terminal.(2)All of the four TPS proteins were successfully expressed in prokaryotic system, but only TPS4 obtained soluble recombinant protein.(3)The purified TPS4 recombinant protein was reacted with GPP, NDP and FPP respectively, and only one product(trans-β-ocimene, β-phellandrene and α-farnesene)was detected. The results provide reference for functional analysis of floral scent related gene at protein level in O. fragrans and for revealing the molecular mechanism of terpenes biosynthesis in plant. [ABSTRACT FROM AUTHOR]

Copyright of Practical Oncology Journal is the property of Journal of Practical Oncology Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Journal of Southern Agriculture is the property of Journal of Southern Agriculture and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)