These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Study of interaction of proton transfer probe 1-hydroxy-2-naphthaldehyde with serum albumins: a spectroscopic study.
    Author: Balia Singh R, Mahanta S, Guchhait N.
    Journal: J Photochem Photobiol B; 2008 Apr 25; 91(1):1-8. PubMed ID: 18296059.
    Abstract:
    In the present work, we have studied the interaction of proton transfer probe 1-hydroxy-2-naphthaldehyde (HN12) with Human Serum Albumin (HSA) and Bovine Serum Albumin (BSA) by steady state absorption and emission spectroscopy combined with time resolved fluorescence measurements. The measured binding constant (K) and free energy change (DeltaG) indicate a stronger affinity of HN12 molecule for HSA than BSA. Steady state anisotropy, excitation anisotropy and fluorescence resonance energy transfer (FRET) studies indicate that the probe molecule resides at the hydrophobic site of the protein environment.
    [Abstract] [Full Text] [Related] [New Search]