Abstract
Using standard methods, the polypeptide α-chain of human haemoglobin A, with the haem group attached, has been prepared and purified. The spectra of the met form and its derivatives have been characterised. The spectrum of the met form of the α-chain is distinctly different from that of methaemoglobin A and closely similar to that of methaemoglobin Norfolk and these spectra shown to be consistent with the existence of two forms of methaemoglobin. Possible structural differences between the two forms are discussed. The formation constant of the azide complex of met α-chain has been measured under different conditions of pH and temperature. The thermodynamic data for the reaction are comparable with those for other methaemoglobins.
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 callDisclaimer: 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.
