噬菌体肽库 meaning in Chinese
phage peptide library
Examples
- Phage display technique and its application in toxoplasma gondii research
噬菌体肽库展示的应用及其最新进展 - Radiolabeling of filamentous phage peptide library with 99mtc and its biodistribution in normal mice
标记丝状噬菌体肽库及其在正常小鼠体内的分布 - The antibody induced by peptide gwyydal abolished vegf - induced huvec growth in dose dependent which specifically express the kdr . moreover , both of the peptide gwyydal and vasavfysalve displaying on phage also inhibited the growth of huvec
[结论]从噬菌体肽库中筛选到了与抗体有高亲和力的阳性噬菌体克隆，噬菌体表达的7 、 12肽gwyydal 、 vasavfysalve模拟了vegf的抗原表位，引起显著的抗- vegf抗体反应。 - In this study , a novel strategy to inhibit the activation of the complement system has been developed . to get the purified clq as the target molecule for biopanning , the first step of our purification was to isolate the clq from clr2cls2 by affinity chromatography on igg - sepharose 4b column
本研究另辟蹊径，以补体经典激活途径始动分子c1q为靶标，采用噬菌体肽库技术，亲和筛选能与c1q结合的噬菌体克隆，研制可抑制补体激活的c1q模拟短肽。 - By elisa analysis , inhibition of binding of clq with the c ! q receptors on u937 cells and competitive inhibition of binding of clq with aggregated immunoglobulin g b y selected phage clones , and dna sequencing , a number of similar , but not identical , sets of sequences of clq - binding clones were identified . the deduced amino acid sequences of selected 9 peptides are wyegpftlytwp , hwdpfslsayfp , ltqhnspffllp , tsnpfflwypqp , qtpfqlw , npfnwts , spfxlts , fltwldp and fstflyp . they show significant efficiency to inhibit the binding of clq with the clq receptors on u937 cells and / or aggregated immunoglobulin g , which suggest that the selected peptides contain the modeling epitopes of clq receptor to bind the collage - like region or igg to bind the head domain of clq
然后，采用噬菌体肽库技术，以c1q为钓饵蛋白，从12肽库和环7肽库中亲和筛选能与c1q结合的噬菌体克隆，经elisa 、 u937细胞配体结合抑制试验、 aigg竞争抑制试验及dna测序，获得了9个具c1q抑制活性克隆的dna序列，其相应的氨基酸序列为： wyegpftlytwp 、 hwdpfslsayfp 、 ltqhnspffllp 、 tsnpfflwypqp 、 qtpfqlw 、 npfnwts 、 spfxlts 、 fltwldp 、 fstflyp ，它们可能模拟c1qr和或igg的c1q结合表位并抑制c1q的活性。