Characterization of a new bradykinin-potentiating peptide (TmF) from Trimeresurus mucrosquamatus
文献类型:期刊论文
作者 | Jia YH1,2; Li DS1; Zhu SW1; Zhang LY1; Ding LS3; Wang WY1; Xiong YL[*]1 |
刊名 | ACTA BIOCHIMICA ET BIOPHYSICA SINICA
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出版日期 | 2003 |
卷号 | 35期号:7页码:619-623 |
关键词 | angiotensin-converting enzyme bradykinin bradykinin-potentiating peptide TmF |
ISSN号 | 0582-9879 |
其他题名 | 湖南烙铁头蛇毒中一个新的舒缓激肽增强肽(TmF) |
通讯作者 | wangwy@mail.kiz.ac.cn |
合作状况 | 其它 |
中文摘要 | 通过 70 %冷甲醇抽提、SephadexG 15分子筛和反相高效液相色谱C1 8层析 ,从湖南产烙铁头蛇毒 (Trimeresurusmucrosquamatus)冻干粉中纯化得到一个新的舒缓激肽增强肽 (BPP) ,命名为TmF。该小肽的氨基酸序列为pGlu Gly Arg Pro Leu Gly Pro Pro Ile Pro Pro (pGlu表示焦谷氨酸 )。序列结果分析表明 ,TmF和已经分离得到的BPPs有很高的序列同源性。MSI MS测定其分子量为 1.110 7kD。TmF的生物学活性和药理学活性检测的结果表明 ,它增强舒缓激肽 (BK) ( 1mg L)诱导的离体豚鼠回肠纵行肌收缩的活性为 ( 1.13± 0 .3)单位 (mg L) ;TmF ( 5 .0× 10 - 4mg kg)可以增强约 ( 14± 2 )mmHg的由BK( 5 .0× 10 - 5mg kg)诱导的舒张压下降 ;在抑制剂试验中 ,不同剂量的TmF和 5× 10 - 2 mg的血管紧张素转化酶保温 30min ,结果表明大约2 .0× 10 - 3mg的TmF表现出对ACE水解活性的半数抑制率 (IC50 )。 |
英文摘要 | A novel bradykinin-potentiating peptide (BPP), designated as TmF, has been purified to homogeneity from the venom of Trimeresurus mucrosquamatus by 70% cold methanol extraction, Sephadex G-15 gel filtration and reverse-phase high performance liquid chromatography (RP-HPLC). The amino acid sequence of TmF was determined to be pGlu-Gly-Arg-Pro-Leu-Gly-Pro-Pro-Ile-Pro-Pro (pGlu denotes pyroglutamic acid), which shared high homology with other BPPs. The molecular mass of TmF was 1.1107 kD as determinated by electrospray ionization-mass spectrometry (ESI-MS), which was in accordance with the calculated value of 1.1106 kD. The potentiating unit of TmF to bradykinin-induced (BK-induced) contraction on the guinea-pig ileum in vitro was (1.13 +/-0.3) unit (mg/L), and TmF (5.0 x10(-4) mg/kg) increased the pressure-lowering-effect of bradykinin (5.0 x10(-5 )mg/kg) with approximate descent value of (14 +/-2) mmHg. In addition, TmF inhibited the conversion of angiotensin I to angiotensin II, 2 x10(-3) mg of TmF caused 50% inhibition (IC(50)) of angiotensin- converting enzyme (ACE) hydrolyzing activity to bradykinin. |
收录类别 | 其他 |
资助信息 | This work was supported by a grant from the Yunnan Y outh Science Foundation of China (No. 1999C0019Q) |
原文出处 | 200335619.pdf |
语种 | 英语 |
公开日期 | 2010-08-24 |
源URL | [http://159.226.149.42:8088/handle/152453/5275] ![]() |
专题 | 昆明动物研究所_其他 昆明动物研究所_动物毒素室 |
作者单位 | 1.Department of Animal Toxinology , Kunming Institute of Zoology , the Chinese Academy of Sciences , Kunming 650223 , China 2.Graduate School of the Chinese Academy of Sciences , Beijing 100009 , China 3.Chengdu Institute of Biology , the Chinese Academy of Sciences , Chengdu 610041 , China |
推荐引用方式 GB/T 7714 | Jia YH,Li DS,Zhu SW,et al. Characterization of a new bradykinin-potentiating peptide (TmF) from Trimeresurus mucrosquamatus[J]. ACTA BIOCHIMICA ET BIOPHYSICA SINICA,2003,35(7):619-623. |
APA | Jia YH.,Li DS.,Zhu SW.,Zhang LY.,Ding LS.,...&Xiong YL[*].(2003).Characterization of a new bradykinin-potentiating peptide (TmF) from Trimeresurus mucrosquamatus.ACTA BIOCHIMICA ET BIOPHYSICA SINICA,35(7),619-623. |
MLA | Jia YH,et al."Characterization of a new bradykinin-potentiating peptide (TmF) from Trimeresurus mucrosquamatus".ACTA BIOCHIMICA ET BIOPHYSICA SINICA 35.7(2003):619-623. |
入库方式: OAI收割
来源:昆明动物研究所
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