Imaging Science and Photochemistry ›› 1994, Vol. 12 ›› Issue (3): 221-228.DOI: 10.7517/j.issn.1674-0475.1994.03.221

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STUDIES OF QUENCHING OF PROTEIN FLUORESCENCE BY SULPHATED HYPOCRELLIN

YUE JIA-CHANG1, DU CHANG-ZHENG1, PANG SU-ZHEN1, AN JING-YI2, JIANG LI-JIN2   

  1. 1. Institue of Biophysics, Academia Sinicca, Beijing 100101, P.R. China;
    2. Institute of Photographic Chemistry, Academia Sinica, Beijing 100101, P.R. China
  • Received:1993-06-25 Revised:1993-09-21 Online:1994-08-20 Published:1994-08-20

Abstract: This papre studies quenching of proteins fluorescence by sulphated Hypocrellin(HA-SO3).The experimental results show that the quenching of protein fluorescence by sul-phated Hypocrellin follows the classical Stern-Volmer equation. The variations of other conditions such as temperatures,viscosities,pH,guanidine-HCl ionic strength were also investigated.The sulphated Hypocrellin is an amphibious molecule with hydrophobic and hydrophilic.The quenching of various proteins may be at different mechanism;The quench fluorescence of protein tryphanyl residues is relatively large rate constant(the Kq values rang from 1-2 × 1013mol/L·s-1).All results also show that HA-SO3 is a more efficientquencher than others.

Key words: fluorescence quenching, protein, hypocrellin