Characterization of the artificially covalent conjugate of B-phycoerythrin and R-phycocyanin and the phycobilisome from Porphyridium cruentum
文献类型：期刊论文
| 作者 | Ma, SY; Wang, GC; Sun, HB; Zeng, CK |
| 刊名 | PLANT SCIENCE
 |
| 出版日期 | 2003-02-01 |
| 卷号 | 164期号:2页码:253-257 |
| 关键词 | B-phycoerythrin (Bpe) R-phycocyanin (Rpc) Bpe-rpc Conjugate Phycobilisome (Pbs) Absorption Spectrum Fluorescence Emission Spectrum |
| ISSN号 | 0168-9452 |
| 文献子类 | Article |
| 英文摘要 | B-phycoerythrin (BPE) and R-phycocyanin (RPC) were purified from Porphyridium cruentum by Sephadex G-200 chromatography, then the BPE was attached covalently to the RPC by reacting their amino groups to form the artificially covalent BPE-RPC conjugate in which the excitation energy can transfer from the BPE to the RPC with low efficiency. Meanwhile, the intact phycobilisome (PBS) consisting of BPE, RPC, APC and L-CM was isolated and purified from Porphyridium cruentum, and the purified PBS was found to keep intact if the solution contains sucrose. Comparison of spectroscopic properties between the purified PBS and the BPE-RPC conjugate suggests that the BPE-RPC conjugate is much more stable than the purified PBS. The construction of BPE-RPC conjugate with low efficiency of the excitation energy transfer may be useful for preparing phycobiliprotein probes. (C) 2002 Elsevier Science Ireland Ltd. All rights reserved.; B-phycoerythrin (BPE) and R-phycocyanin (RPC) were purified from Porphyridium cruentum by Sephadex G-200 chromatography, then the BPE was attached covalently to the RPC by reacting their amino groups to form the artificially covalent BPE-RPC conjugate in which the excitation energy can transfer from the BPE to the RPC with low efficiency. Meanwhile, the intact phycobilisome (PBS) consisting of BPE, RPC, APC and L-CM was isolated and purified from Porphyridium cruentum, and the purified PBS was found to keep intact if the solution contains sucrose. Comparison of spectroscopic properties between the purified PBS and the BPE-RPC conjugate suggests that the BPE-RPC conjugate is much more stable than the purified PBS. The construction of BPE-RPC conjugate with low efficiency of the excitation energy transfer may be useful for preparing phycobiliprotein probes. (C) 2002 Elsevier Science Ireland Ltd. All rights reserved. |
| 学科主题 | Biochemistry & Molecular Biology ; Plant Sciences |
| 语种 | 英语 |
| WOS记录号 | WOS:000180838400014 |
| 公开日期 | 2010-12-22 |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/3259]  |
| 专题 | 海洋研究所_实验海洋生物学重点实验室 |
| 作者单位 | Acad Sinica, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China |
| 推荐引用方式 GB/T 7714 | Ma, SY,Wang, GC,Sun, HB,et al. Characterization of the artificially covalent conjugate of B-phycoerythrin and R-phycocyanin and the phycobilisome from Porphyridium cruentum[J]. PLANT SCIENCE,2003,164(2):253-257. |
| APA | Ma, SY,Wang, GC,Sun, HB,&Zeng, CK.(2003).Characterization of the artificially covalent conjugate of B-phycoerythrin and R-phycocyanin and the phycobilisome from Porphyridium cruentum.PLANT SCIENCE,164(2),253-257. |
| MLA | Ma, SY,et al."Characterization of the artificially covalent conjugate of B-phycoerythrin and R-phycocyanin and the phycobilisome from Porphyridium cruentum".PLANT SCIENCE 164.2(2003):253-257. |
入库方式： OAI收割
来源：海洋研究所
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