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Identification and characterization of Laodelphax striatellus (Insecta: Hemiptera: Delphacidae) neutral sphingomyelinase

文献类型：外文期刊

第一作者： Zhou, Y.

作者： Zhou, Y.;Lin, X. -W.;Begum, M. -A.;Zhang, C. -H.;Shi, X. -X.;Jiao, W. -J.;Zhang, Y. -R.;Zhu, Z. -R.;Zhou, Y.;Lin, X. -W.;Begum, M. -A.;Zhang, C. -H.;Shi, X. -X.;Jiao, W. -J.;Zhang, Y. -R.;Zhu, Z. -R.;Zhou, Y.;Lin, X. -W.;Begum, M. -A.;Zhang, C. -H.;Shi, X. -X.;Jiao, W. -J.;Zhang, Y. -R.;Zhu, Z. -R.;Zhou, Y.;Yuan, J. -Q.;Li, H. -Y.;Yang, Q.;Mao, C.

作者机构：

关键词： sphingomyelinase;Laodelphax striatellus;sphingolipid;insect

期刊名称：INSECT MOLECULAR BIOLOGY （影响因子：3.585；五年影响因子：3.215 ）

ISSN：

年卷期：

页码：

收录情况： SCI

摘要： The neutral sphingomyelinase (nSMase) 1 homologue gene LsSMase was cloned from Laodelphax striatellus, a direct sap-sucker and virus vector of gramineous plants, and expressed via a Bac to Bac baculovirus expression system. The LsSMaseenhanced green fluorescent protein fusion protein was located in the endoplasmic reticulum in a similar manner to mammalian nSMase 1. The biochemical properties of LsSMase were determined in detail. The optimal pH and temperature for recombinant LsSMase were 8 and 37 degrees C, respectively. LsSMase was an Mg2+ or Mn2+ dependent enzyme, but different concentration of each were needed. The activity of LsSMase was significantly stimulated by Ethylene glycol bis(2-aminoethyl ether) tetraacetic acid ( EGTA), whereas it was inhibited by ethylenediaminetetraacetic acid. Millimolar concentrations of Zn2+ completely inhibited LsSMase. The reducing agents dithiothreitol and beta-mercaptoethanol varied in their effects on activity. Phospholipids were not found to stimulate LsSMase.

分类号： R47

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