Bilirubin binding properties of pigeon serum albumin and its comparison with human serum albumin.
Binding of bilirubin (BR) to pigeon serum albumin (PgSA) was studied by absorption, fluorescence and CD spectroscopy and results were compared with those obtained with human serum albumin (HSA). PgSA was found to be structurally similar to HSA as judged by near- and far-UV CD spectra. However, PgSA lacks tryptophan. Binding of BR to PgSA showed relatively weaker interaction compared to HSA in terms of binding affinity, induced red shift in the absorption spectrum of BR and CD spectral characteristics of BR-albumin complexes. Photoirradiation results of BR-albumin complexes also showed PgSA-bound BR more labile compared to HSA-bound BR.
Khan
Mateen A
MA
Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh 202 002, India.
Kumar
Yogesh
Y
Tayyab
Saad
S
D000818:Animals; D001663:Bilirubin / Q000378:metabolism*; D002942:Circular Dichroism; D010856:Columbidae / Q000097:blood*; D006801:Humans; D008027:Light; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism* / Q000528:radiation effects; D013045:Species Specificity; D013050:Spectrometry, Fluorescence; D014364:Tryptophan / Q000737:chemistry
D012709:Serum Albumin; D014364:Tryptophan; D001663:Bilirubin