کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9884692 | 1537059 | 2005 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Evidence for dissociation of chlorophyll b from the main light-harvesting complex in the oligomerization state isolated from marine alga, Bryopsis corticulans
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کلمات کلیدی
OligomerizationChlRP-HPLCn-octyl-β-d-glucopyranosidesodium dodecyl sulfate-polyacrylamide gel electrophoresis - الکتروفورز ژل دوده سولفات سدیم پلی آکریل آمیدSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدLHC - برخورد دهنده بزرگ هادرون circular dichroism - رنگ تابی دورانیChlorophyll - سبزینه یا کلروفیلSpectroscopy - طیفسنجیLight-harvesting complex - مجتمع جمع آوری نورreversed-phase high performance liquid chromatography - کروماتوگرافی مایع با کارایی بالا با فاز برگشت پذیر
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Evidence for dissociation of chlorophyll b from the main light-harvesting complex in the oligomerization state isolated from marine alga, Bryopsis corticulans Evidence for dissociation of chlorophyll b from the main light-harvesting complex in the oligomerization state isolated from marine alga, Bryopsis corticulans](/preview/png/9884692.png)
چکیده انگلیسی
We investigated the composition and organization of chlorophylls in monomers, trimers and oligomers (small aggregates) of the main light-harvesting complex (LHC II) isolated from marine alga, Bryopsis corticulans, using a combination of measurements with reversed-phase high performance liquid chromatography (RP-HPLC) and steady-state spectroscopy of absorption, circular dichroism (CD) and low temperature fluorescence. The composition and organization of the chlorophylls in monomeric and trimeric LHC II were essentially identical to those of LHC II from higher plants. For LHC II oligomers, a large decrease of chlorophyll (Chl) b absorption and of CD signals corresponding to Chl b was consistent with the quantitative analysis of Chl b by RP-HPLC, indicating that oligomerization of the LHC II proteins significantly influenced spectroscopic properties and led to the dissociation of Chl b molecules from LHC II. Our data strongly suggested that protein oligomerization constitutes a structural basis for the decrease of Chl b molecules in LHC II of B. corticulans. The LHC II of B. corticulans might play a photoprotective role with the reduction of the ability of light absorption via alteration of its own structural conformation.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1707, Issues 2â3, AprilâMay 2005, Pages 170-178
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1707, Issues 2â3, AprilâMay 2005, Pages 170-178
نویسندگان
Hui Chen, Shihua Shen, Yu Liang, Jing Leng, Mingjuan Tang, Yandao Gong,