Quantitative estimation of native and treated with 4% formaldehyde albumin, pepsin, lysozyme, histone, gelatin and other proteins was carried out using four procedures--biurete, Lowry-Folin, ninhydrin and coomassy R-250. Chromogeneity of proteins in corresponding color reactions was expressed as OD per 100 micrograms of nitrogen estimated by means of Kjeldahl micromethod. The proteins were treated with formaldehyde in corresponding buffers at 20 degrees within 7 days, non-bound or loosely bound formaldehyde was dialysed. Native proteins were dissimilar in their chromogeneity; these differences were the highest for Lowry-Folin and coomassy procedures. Formalinization affected the protein chromogenencity depending on a protein nature, conditions of formaldehyde treatment and on the procedure of estimation used. As shown by analysis of the data obtained the alterations of chromogeneity did not reflect the rate of reactive group blocking by formaldehyde in a protein molecule. The quantitative methods should be used very carefully in estimation of formalinized proteins.