研究报告 |
|
|
|
|
中国林蛙核糖核酸酶Rdrlec新基因的原核可溶表达 |
陶凤云, 尹雪薇, 李丹, 蒋丹, 赵伟 |
北京联合大学生物化学工程学院 北京 100023 |
|
Prokaryotic Soluble Expression of a Novel Ribonuclease Gene Rdrlec from Rana dybowskii |
TAO Feng-yun, YIN Xue-wei, LI Dan, JIANG Dan, ZHAO Wei |
Biochemical Engineering College of Beijing Union University, Beijing 100023, China |
引用本文:
陶凤云, 尹雪薇, 李丹, 蒋丹, 赵伟. 中国林蛙核糖核酸酶Rdrlec新基因的原核可溶表达[J]. 中国生物工程杂志, 2013, 33(1): 27-32.
TAO Feng-yun, YIN Xue-wei, LI Dan, JIANG Dan, ZHAO Wei. Prokaryotic Soluble Expression of a Novel Ribonuclease Gene Rdrlec from Rana dybowskii. China Biotechnology, 2013, 33(1): 27-32.
链接本文:
https://manu60.magtech.com.cn/biotech/CN/
或
https://manu60.magtech.com.cn/biotech/CN/Y2013/V33/I1/27
|
[1] Leone E, D’Alessio G. Structure and properties of seminal ribonuclease. Biochem Soc Trans, 1977,5 (2):466-470. [2] Beintema J J, Gaastra W, Lenstra J A, et al. The molecular evolution of pancreatic ribonuclease. J Mol Evol, 1977,10 (1):49-71. [3] Pizzo E, Buonanno P, Di Maro A, et al. Ribonucleases and angiogenins from fish. J Biol Chem, 2006,281 (37):27454-27460. [4] Ardelt W, Mikulski S M, Shogen K. Amino acid sequence of an anti-tumor protein from Rana pipiens oocytes and early embryos. Homology to pancreatic ribonucleases. J Biol Chem, 1991,266 (1):245-251. [5] Beintema J J, Broos J, Meulenberg J, et al. The amino acid sequence of snapping turtle (Chel·ra serpentina) ribonuclease. Eur J Biochem, 1985,153 (2):305-312. [6] Nitto T, Dyer K D, Czapiga M, et al. Evolution and function of leukocyte RNase A ribonucleases of the avian species, Gallus gallus. J Biol Chem, 2006,281 (35):25622-25634. [7] Zhu C F, Liu Q, Zhang L, et al. RNase9, an androgen-dependent member of the RNase A family, is specifically expressed in the rat epididymis. Biol Reprod, 2007,76 (1):63-73. [8] 陶凤云,赵伟,马润宇. 核糖核酸酶A超家族成员杀菌作用研究进展. 中国抗生素杂志,2009,34(6):321-325, 379. Tao F Y, Zhao W, Ma R Y. Progress in bacterictdal activity of ribonuclease A superfamily menbers. Chinese Journal of Antibiotics, 2009, 34(6): 321-325, 379. [9] Monti D M, Yu W, Pizzo E, et al. Characterization of the angiogenic activity of zebrafish ribonucleases. FEBS J, 2009,276 (15):4077-4090. [10] Lee I. Ranpirnase (Onconase), a cytotoxic amphibian ribonuclease, manipulates tumour physiological parameters as a selective killer and a potential enhancer for chemotherapy and radiation in cancer therapy. Expert Opin Biol Ther, 2008,8 (6):813-827. [11] Bradford M M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical biochemistry,1976, 72:248-254. [12] Rosenberg H F. Recombinant human eosinophil cationic protein. Ribonuclease activity is not essential for cytotoxicity. J Biol Chem, 1995,270 (14):7876-7881. [13] Ardelt W, Shogen K, Darzynkiewicz Z. Onconase and amphinase, the antitumor ribonucleases from Rana pipiens oocytes. Curr Pharm Biotechnol, 2008,9 (3):215-225. [14] Liao Y D, Huang H C, Leu Y J, et al. Purification and cloning of cytotoxic ribonucleases from Rana catesbeiana (bullfrog). Nucleic Acids Res, 2000,28 (21):4097-4104. [15] 陶凤云,赵伟,林强,等. 中国林蛙卵核糖核酸酶的分离纯化及其抗肿瘤作用. 中国生物工程杂志, 2010, 30(5):103-109. Tao F Y, Zhao W, Lin Q, et al. Algtotoxic ribonucleose isolated from occytes of Chinese Nothease Frog Rana dybowckii. China Biotechnology, 2010,30(5):103-109. [16] Tao F, Fan M, Zhao W, et al. A novel cationic ribonuclease with antimicrobial activity from Rana dybowskii. Biochem Genet, 2011, 49(5-6): 369-384. [17] Lou Y C, Huang Y C, Pan Y R, et al. Roles of N-terminal pyroglutamate in maintaining structural integrity and pKa values of catalytic histidine residues in bullfrog ribonuclease 3. J Mol Biol, 2006,355 (3):409-421. [18] Gorbatyuk V Y, Tsai C K, Chang C F, et al. Effect of N-terminal and Met23 mutations on the structure and dynamics of onconase. J Biol Chem, 2004,279 (7):5772-5780. [19] Leland PA, Schultz L W, Kim B M, et al. Ribonuclease A variants with potent cytotoxic activity. Proc Natl Acad Sci U S A, 1998,95 (18):10407-10412. [20] Gagliardo B, Faye A, Jaouen M, et al. Production of biologically active forms of recombinant hepcidin, the iron-regulatory hormone. FEBS J, 2008, 275:3793-3803. [21] Stewart E J, Aslund F, Beckwith J. Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins. The EMBO journal, 1998, 17:5543-5550. |
|
Viewed |
|
|
|
Full text
|
|
|
|
|
Abstract
|
|
|
|
|
Cited |
|
|
|
|
|
Shared |
|
|
|
|
|
Discussed |
|
|
|
|