[The oxygen-binding properties of hemoglobin modified by the action of temperature and sodium dodecyl sulfate].
Oxygen-binding properties of mice hemoglobin modified by temperature (20-45 degrees C) or by this temperature together with sodium dodecyl sulphate (SDS) of different concentrations (3.47 x 10(-5)-3.47 x 10(-4) M) were studied by means of spectrophotometry. The increase of temperature up to 42-45 degrees C resulted in accumulation of the hemoglobin aggregates larger than tetramers. The combined effect of SDS and temperature may change the protein microenvironment as well as to integrate the hemoprotein molecules into subunits, depending upon the SDS concentration.
Artiukhov
V G
VG
Vashanov
G A
GA
D000818:Animals; D006454:Hemoglobins / Q000032:analysis / Q000187:drug effects / Q000378:metabolism*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D051379:Mice; D010100:Oxygen / Q000097:blood*; D010108:Oxyhemoglobins / Q000032:analysis / Q000187:drug effects / Q000378:metabolism; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology*; D012996:Solutions; D013053:Spectrophotometry; D013696:Temperature
D006454:Hemoglobins; D010108:Oxyhemoglobins; D012996:Solutions; D012967:Sodium Dodecyl Sulfate; D010100:Oxygen
Kislorodsviazyvaiushchie svoĭstva gemoglobina, modifitsirovannogo vozdeĭstviem temperatury i dodetsilsul'fata natriia.