Formaldehyde-induced modification of hemoglobin in vitro.
Formaldehyde is known to react with proteins. The purpose of our experiments was to analyse in vitro the effect of formaldehyde on the physicochemical and biological properties of hemoglobin molecules. The effect of formaldehyde concentration, reaction time, pH and temperature on hemoglobin free amino groups was estimated. The modified hemoglobin was analysed using electrophoretic, potentiometric and spectrophotometric techniques. Reaction between formaldehyde and hemoglobin was accelerated by increasing concentration of formaldehyde and higher temperature. This reaction was most intensive during the first few hours at pH 7.4 so the amount of free amino groups of hemoglobin was significantly diminished by directly mixing formaldehyde with hemoglobin. The modified protein was characterized by the increase in electrophoretic mobility and the decrease in maximum absorption derived from porphyrin rings. Formaldehyde modified hemoglobin was less susceptible to the action of cathepsin D.
Farbiszewski
R
R
Department of Analytical Chemistry, Medical University, Bialystok, Poland.
Skrzydlewska
E
E
Roszkowska
A
A
D002402:Cathepsin D / Q000378:metabolism; D005557:Formaldehyde / Q000378:metabolism*; D006454:Hemoglobins / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D013056:Spectrophotometry, Ultraviolet
D006454:Hemoglobins; D005557:Formaldehyde; D002402:Cathepsin D