Literature DB >> 8005348

Binding of meso-tetra(4-sulfonatophenyl)porphine to haemopexin and albumin studied by spectroscopy methods.

J Bartosová1, I Kalousek, Z Hrkal.   

Abstract

1. The interaction of haemopexin and albumin with TPPS4 was studied by measuring the absorption and fluorescence spectra. Haemopexin was found to have one strong TPPS4 binding center (Ka = 3 x 10(7) M-1). 2. Haem-haemopexin complex appears to have no specific binding site for TPPS4. Occupation of the specific binding center of haemopexin molecule by a haem abolishes TPPS4 binding. 3. Albumin was found to possess one strong TPPS4 binding center (Ka = 3 x 10(6) M-1) besides two or three weak binding sites (Ka = 2 x 10(5) M-1). 4. Haem-albumin complex possesses only one weak TPPS4 binding site (Ka = 7 x 10(5) M-1). These observations suggest identity of primary binding sites of TPPS4 and haem on albumin molecule.

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Year:  1994        PMID: 8005348     DOI: 10.1016/0020-711x(94)90162-7

Source DB:  PubMed          Journal:  Int J Biochem        ISSN: 0020-711X


  2 in total

1.  The influence of human serum albumin on the photogeneration of singlet oxygen by meso-tetra(4-sulfonatophenyl)porphyrin. An infrared phosphorescence study.

Authors:  M Korínek; R Dedic; A Molnár; J Hála
Journal:  J Fluoresc       Date:  2006-02-09       Impact factor: 2.217

2.  STRUCTURE OF PORPHYRIN TPPS4 AND ITS INTERACTION WITH METAL IONS AS ELUCIDATED BY 1H NMR AND UV-VISIBLE SPECTRA.

Authors:  Zhiyan Song; Adegboye O Adeyemo; Jannie Baker; Shakeya M Traylor; Marcia L Lightfoot
Journal:  Ga J Sci       Date:  2011
  2 in total

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