Radiation induced structural and functional modification of haemoglobin.
An abnormality in the primary structure of dog haemoglobin was observed 1-20 days after their whole body irradiation with 190 keV X-rays (4.0 Gy). It consisted in a substitution of tryptophane residue in position 15 of the beta-chain for serine. The percentage of abnormal beta-chains in different time intervals after irradiation was determined. The structural changes have functional impact: an increasing haemoglobin affinity to oxygen. This could be explained on the basis of changes in the tertiary structure of haemoglobin, which may result from the substitution Trp 15----Ser15 in the beta-chain which may influence the haeme ability to bind oxygen.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D004285:Dogs; D005914:Globins / Q000032:analysis / Q000528:radiation effects; D006454:Hemoglobins / Q000378:metabolism / Q000528:radiation effects*; D010100:Oxygen / Q000378:metabolism; D010455:Peptides / Q000032:analysis; D011487:Protein Conformation / Q000528:radiation effects; D014357:Trypsin; D014916:Whole-Body Irradiation
D000596:Amino Acids; D006454:Hemoglobins; D010455:Peptides; D005914:Globins; D014357:Trypsin; D010100:Oxygen