期刊
JOURNAL OF INSECT PHYSIOLOGY
卷 49, 期 1, 页码 1-9出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/S0022-1910(02)00189-0
关键词
virus-like particle-protein; phospholipid hydroperoxide glutathione peroxidase; Venturia canescens; Drosophila melanogaster
We compared the functional properties of two insect members of the phospholipid hydroperoxide glutathione peroxidases (PHGPx) family, VLP1, a major component of virus-like particles from the hymenopteran endoparasitoid Venturia canescens and its closest Drosophila relative, one of the putative PHGPx-proteins predicted from the Berkeley Drosophila genome sequence project. Recombinant Drosophila PHGPx shows enzymatic activity towards a number of PHGPx substrates, while the recombinant PHGPx-like domain of VLP1 lacks a functionally relevant cysteine and enzyme activity. A possible function of a non-enzymatic extracellular PHGPx-like protein is discussed. (C) 2002 Elsevier Science Ltd. All rights reserved.
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