Abstract
The binding of bilirubin to erythrocytes of several mammalian species, i.e. human, buffalo, goat and sheep was studied. In all cases, curves between bilirubin desorbed from erythrocytes and bilirubin in the incubate followed Michaelian saturation kinetics. The dissociation constants of the bilirubin-receptor complex and saturable binding sites were calculated using double reciprocal plots. Goat erythrocytes had the highest dissociation constant (265.7 mumol/l) and highest saturation (125.9 microM), whereas sheep erythrocytes had the lowest dissociation constant (115.6 mumol/l) and lowest saturation (62.5 microM). Buffalo and human erythrocytes bound bilirubin in a similar fashion, and the values of interaction parameters were midway between those obtained with goat and sheep erythrocytes. Differences in the affinity and number of saturable binding sites can be attributed to the different make-up of the erythrocyte membranes of these species.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Comparative biochemistry and physiology. Part A, Physiology
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
