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Identification and characterization of Laodelphax striatellus (Insecta: Hemiptera: Delphacidae) neutral sphingomyelinase.
- Source :
-
Insect molecular biology [Insect Mol Biol] 2017 Aug; Vol. 26 (4), pp. 392-402. Date of Electronic Publication: 2017 Apr 04. - Publication Year :
- 2017
-
Abstract
- 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 LsSMase-enhanced 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 °C, respectively. LsSMase was an Mg <superscript>2+</superscript> or Mn <superscript>2+</superscript> 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 Zn <superscript>2+</superscript> completely inhibited LsSMase. The reducing agents dithiothreitol and β-mercaptoethanol varied in their effects on activity. Phospholipids were not found to stimulate LsSMase.<br /> (© 2017 The Royal Entomological Society.)
Details
- Language :
- English
- ISSN :
- 1365-2583
- Volume :
- 26
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Insect molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 28374513
- Full Text :
- https://doi.org/10.1111/imb.12302