Biotechnology

Permanent URI for this community

http://dspace.alquds.edu:4000/handle/20.500.12213/75
Biotechnology

Browse

Browsing Biotechnology by Author "Abu Teir, M. M."

Now showing 1 - 2 of 2
  • Thumbnail Image
    Item
    Spectroscopic approach of the interaction study of Ceftriaxone and human serum albumin
    (Academic Journals, 2013-12-10) Abu Teir, M. M.; Ghithan, J.; Abu-Taha, M. I.; Darwish, S. M.; Abu-hadid, M. M
    Under physiological conditions, interaction between ceftriaxone and human serum albumin was investigated by using fluorescence spectroscopy and ultra violet (UV) absorption spectrum. From spectral analysis, ceftriaxone showed a strong ability to quench the intrinsic fluorescence of human serum albumin (HSA) through a static quenching procedure. The binding constant (k) is estimated as K=1.02× 103 M-1 at 298 K. Fourier transform infrared spectroscopy (FT-IR) spectroscopy with Fourier self-deconvolution technique was used to determine the protein secondary structure and drug binding mechanisms. The observed spectral changes indicated the formation of H-bonding between ceftriaxone and HSA molecules at higher percentage for -helix than for the -sheets.
  • Thumbnail Image
    Item
    Study of Progesterone interaction with Human Serum Albumin: Spectroscopic approach
    (2011-01-17) Abu Teir, M. M.; Ghithan, J. H.; Darwish, S. M.; Abu-Hadid, M. M.
    The interaction between progesterone and human serum albumin has been investigated. This interaction was studied by UV-absorption and fluorescence spectroscopy. From spectral analysis progesterone showed a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. The binding constant (K) is estimated 6.56×102 M-1 at 293 K. FT-IR spectroscopy with Fourier self-deconvolution technique was used to determine HSA secondary structure and progesterone binding mechanisms. The observed spectral changes indicate the formation of H-bonding between progesterone and HSA molecules which can be related to the intensity decrease in the absorption band of α-helix relative to that of β-sheets.