Tin tetrachloride interaction with human hemoglobin.
In the presence of tin tetrachloride, the rate constant for the rebinding of CO to the triliganded hemoglobin, l'4, is much increased and the number of molecules participating in the CO ligation is decreasing. The pH drops, but a proton consumption process also takes place at the same time. The heme and its environment do not seem to change much, but the tin complexing to protein is very probable. The oxidation of hemoglobin in the form of either oxy or carbonmonoxy occurs with rather high rate.
Frunza
L
L
Institute of Physics and Technology of Materials, Bucharest-Magurele, Romania.
Serbanescu
R M
RM
D002248:Carbon Monoxide / Q000378:metabolism; D002263:Carboxyhemoglobin / Q000378:metabolism; D006454:Hemoglobins / Q000187:drug effects* / Q000378:metabolism / Q000528:radiation effects; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007834:Lasers; D008024:Ligands; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism; D010108:Oxyhemoglobins / Q000378:metabolism; D010782:Photolysis; D011485:Protein Binding / Q000187:drug effects; D017971:Tin Compounds / Q000494:pharmacology*
D006454:Hemoglobins; D008024:Ligands; D010108:Oxyhemoglobins; D017971:Tin Compounds; C041694:stannic chloride; D002248:Carbon Monoxide; D002263:Carboxyhemoglobin; D010100:Oxygen