Paper Titles

Direct Observation of Hydroxyapatite Nanoparticles In Vivo
p.688

Effects of Working Pressure on the Microstructure and Properties of ZnO Thin Films Prepared by DC Magnetron Sputtering
p.692

The Analysis of the Interface States of Low-Density Materials in the Forming Process
p.696

Research on Properties of Automobile Lubricant Containing Nano-Ceramic Additives
p.700

Effect of N⁺Ion Beam Exposure on the Secondary Structure of Horseradish Peroxidase
p.705

Research Development of Residual Stress Determination with Generalized Stress Increment Testing Method
p.709

Ultrasonic Fatigue Tests on a High Strength Steel for Welded Structure
p.714

Experimental Research on Ultrasonic Vibration Turning of Finish Machining Technology
p.718

Finite Element Analysis of Flexural Strength for Helical Gear of Automotive Transmission
p.723

HomeAdvanced Materials ResearchAdvanced Materials Research Vols. 503-504Effect of N+ Ion Beam Exposure on the Secondary...

Effect of N⁺Ion Beam Exposure on the Secondary Structure of Horseradish Peroxidase

Article Preview

Abstract:

After the horseradish peroxidase (HRP) was treated with different dose of N+ ion beam, the effect of N+ ion beam on the secondary structure of HRP was studied by FTIR(Fourier-transformation infrared spectroscopy). The results have shown that different dose ranging from 1015 to 1016 ions/cm2 has different effects on the secondary structure contents the HRP. The N+ implantation induce the mutual change in the secondary structure unit of HRP. It was suggested that N+ ion beam was bound to result in conformational change.

You might also be interested in these eBooks

Frontiers of Manufacturing Science and Measuring Technology II

Info:

Periodical:

Advanced Materials Research (Volumes 503-504)

Pages:

705-708

DOI:

https://doi.org/10.4028/www.scientific.net/AMR.503-504.705

Citation:

Cite this paper

Online since:

April 2012

Authors:

Qiang Xu

Keywords:

Activity, Horseradish Peroxidase (HRP), N⁺ Ion Beam, Secondary Structure

Export:

RIS, BibTeX

Price:

Permissions CCC:

Request Permissions

Permissions PLS:

Request Permissions

Сopyright:

© 2012 Trans Tech Publications Ltd. All Rights Reserved

Share:

Citation:

[1] Z. L. Yu, Y. J. Wu, J. G. Deng, J. L He, Y. P. Huo, Y. J. Wu, X. D. Wang, G. F. Lui. Nucl. Instru. Meth. Phys. Res., Vol. 59(1991), p.705–708.

[2] J. B. Yang, L. J. Wu, J. D. Wu, Y. J. Wu, Z. L. Yu, Z. H. Xu. Chinese science bulletin, Vol. 40(1995), p.427–431.

[3] D. J. Song, Z. L. Yu. Plasma Science and Technology Plasma Science and Technology, Vol. 2(2000), p.415–421.

[4] C. L. Shao, X. Q. Wang, Z. L. Yu. Radiat Phys. Chem., Vol. 50(1997), p.561–565.

[5] Z. L. Yu, C. L. Shao. Radiat Phys Chem., Vol. 43(1994), p.349–351.

[6] W. D. Huang, Z. L. Yu, Y. H. Zhang. Chemical Physics, Vol. 237(1998), p.223–231.

[7] K. Chattopadhyay, S. Mazumdar. Biochemistry, Vol. 39(2000), p.263–270.

[8] M. Gajhede, D. J. Schuller, A. Henriksen. Nat. Struct. Biol., Vol. 4(1997), p.1032–1038.

[9] V. Thanabal, J. S. de Ropp, G. N. LaMar.J. Am. Chem. Soc., Vol. 110(1998), p.3027–3035.

[10] M. Jackson, H. H. Mantsch. Crit. Rev. Biochem. Mol. Biol., Vol. 30(1995), pp.95-120.

[11] T.E. Creighton. Proteins: Structure and Molecular Properties (W H Freeman and Company, New York 1993).

[12] P. I. Haris, Chapman D. Trends Biochem Sci., Vol. 17(1992), p.328–333.

[13] D. M. Byler, J. N. Brouille, H. Susi. Spectroscopy, Vol. 1(1986), p.29–32.

[14] H. Susi, D. M. Byler. Methods Enzymol., Vol. 130(1986), p.290–311.

[15] M. Hollosi, Z. Majer, A. Z. Ronai. Biopolymers, Vol. 34(1994), p.177–85.