Binding of photobilirubin to human serum albumin. Estimate of the affinity constant.

Abstract

Results of experiments based upon circular dichroic spectra suggest that configurationally (Z leads to E) isomerized bilirubin (photobilirubin) binds to human serum albumin at the primary bilirubin binding site with an affinity only 2-3 times lower than that of bilirubin. The high affinity of photobilirubin for albumin, comparable to that of bilirubin, supports the roles of albumin in the stabilization and transport of the isomerized pigment in vivo and strongly suggests that albumin also functions to sequester photobilirubin effectively, reducing its toxic potential. The high affinity of photobilirubin for albumin predicts that the isomerized pigment, formed in large amounts during phototherapy for neonatal hyperbilirubinemia, should not appear in the fast-diazo-reacting ('direct') bilirubin pool nor should it interfere with nonspectroscopic bilirubin binding tests. These predictions were confirmed for the Evelyn and Malloy diazo assay for 'direct' bilirubin and a Sephadex chromatography method for assessing 'loosely bound' plasma bilirubin.

• Authors: A A Lamola, J Flores, W E Blumberg
• Journal: European journal of biochemistry (Eur J Biochem) Vol. 132 Issue 1 Pg. 165-9 (Apr 15 1983) ISSN: 0014-2956 [Print] England
• PMID: 6840080 (Publication Type: Journal Article)

Chemical References

• Serum Albumin
• photobilirubin
• Bilirubin

Topics

• Bilirubin (blood)
• Binding Sites
• Circular Dichroism
• Humans
• Protein Binding
• Serum Albumin (metabolism)
• Stereoisomerism