Effect of Fibrinolytic Compound GDG on Crystal Structure of Lysozyme

Abstract:

Lysozyme was extensively studied as a model of protein crystallization, we identified that 15 mg/ml lysozyme, 0.1 M sodium acetate buffer containing 5% (w/v) sodium chloride and 0.02% (w/v) sodium azide, pH 5.2, crystal nucleus were less and crystals could reach a certain size. Basic on GDG effected conformation of enzyme which enhancing the reciprocal activation of plasminogen and prourokinase via the elevation of intrinsic activity of prourokinase, we obtained the crystal of lysozyme added α-D-glucopyranoslydiacylglycerol (GDG), GDG: HEWL (c/c) = 2:1, 1:1, 1:2, performed the synchrotron radiation diffraction and collected the three dimensional structure data. It is showing that increased in number of crystal amount and decreased in volume of crystal size in crystallization of lysozyme accompanied by the concentration of GDG. It is not displayed effect on the main chain and most side chains of lysozyme in the presence of GDG in the electron density map.

• Periodical: Advanced Materials Research (Volumes 554-556)
• Pages: 1768-1775
• DOI: https://doi.org/10.4028/www.scientific.net/AMR.554-556.1768
• Online since: July 2012
• Authors: Yong Xian Wang*, Wen Hui Wu, Bin Bao, Rui Rui Song, Li Chun Sun
• Keywords: Crystal Structure, GDG, Lysozyme, Protein Crystallization

References

[1] A. McPherson: Methods Vol. 34 (2004), p.254.

[2] Xinxin Li, Xiaodong Xu, Yuanyuan Dan and Milin Zhang: Biotechnol. Bull Vol. 6 (2007), p.44. (In Chinese)

[3] E.H. Snell, T.J. Boggon, J.R. Helliwell, M.E. Moskowitz and A.N.E. Nadarajah: Acta Cryst. D Biol. Cryst Vol. 53(1997), p.747

DOI: 10.1107/s0907444997007968

[4] P.D. Collingsworth, T.L. Bray and G.K. Christopher: J. Cryst. Growth Vol. 219 (2000), p.283.

[5] M.Y. Gamarnik: J. Cryst. Growth Vol. 197 (1999), p.254.

[6] Longguang Jiang, Haiuang Yu, Cai Yuan, Jundong Wang, Licing Chen, E.J. Meehan, Zixiang Huang and Mingdong Huang: Chin. J. Struct. Chem Vol. 28 (2009), p.1427.

[7] S. Glen, P. Christopher, N.K. Ursula, P.P. Christopher, S. Derek, D.M. Christopher, S.I. David and J.Y. E: Structure Vol. 3 (1995), p.581.

[8] Xiaoqiang Wang, T. Jordan, H. Bret and Xuejun C. Zhang: FEBS Lett Vol.459 (1999), p.85.

[9] F.B. William: Fibrinolysis Vol.7 (1993), p.38.

[10] E. Stefanie, S. Wolf-Dieter, B. Simone, H. Sven and H.W. Dirk: J.Mol.Biol Vol. 343 (2004), p.997.

[11] Ya Shu, Wenhui Wu, Zhihe Wang and Bin Bao: J. Food Sci Vol. 28 (2007), p.471. ( In Chinese)

[12] Fei Hao, Wenhui Wu, Jiahua Qu and Bin Bao: Chin. J. Mar. Drugs Vol. 29 (2010), p.6. ( In Chinese)

[13] Wenhui Wu, N. Ritsuko, M. Fumihiko and H. Keiji: Biosci. Biotechnol. Biochem Vol.68 (2004), p.1549.

[14] Jie Lu, Xiujuan Wang and Chibun Ching: Prog. Cryst. Growth. Ch Vol. 45 (2002), p.201.

[15] J.H. Christopher, N.M. Sean and S.R. Dean: Dartm. Undergr. J.Sci Vol. 1 (2000), p.30.

[16] S.D. Durbin and G. Feher: J. Cryst. Growth Vol.76 (1986), p.583.

[17] Hailiang Cui, Yong Yu, Wanchun Chen and Qi Kang.: Chin. Chem. Lett Vol.17 (2006), p.101.

[18] S. David, O'M. Carolyn and C. Miquel: Biochem. Educ Vol. 26 (1998), p.173.

[19] Fengyun Tao, Xinmiao Zhang and Runyu Ma: Chem. Ind. Eng Vol. 20 (2006), p.37. ( In Chinese)

[20] K. Hengming, Ch. Yuxiang and C. Jiweni, in: X-ray crystallography of biomacromolecules, chapter, 12, Chemical Industry Publishers (2010).

[21] Fei Hao, Wenhui Wu, Jiahua Qu and Bin Bao: Spectrosc. Spect. Anal Vol. 30 (2010), p.2171. ( In Chinese)