From 7 to 8 minor fractions were isolated from normal and pathologically altered human blood serum albumin by means of isoelectric focusing in borate-polyol system. As distinct from the whole albumin molecule, these minor fractions contained 12-14% carbohydrates, I-1.2% of which were linked by covalent bonds while the rest of it were absorbed. The fractions included a number of amides, amount of which was gradually elevated with an increase in the isoelectric point. As shown by circular dichroism studies content of alpha-spirals decreased from 20% to 5% in the proteins, depending on the pI value. Spontaneous deamidation was noted during storage. Normally the content of these proteins constituted from 3% to 4%; in liver cirrhosis it might increase up to 50%.