The adsorption of tripsin and albumin on silicapolymetylsilocsan (SG-PMS) and its modified forms by cooper (II)--(SG-PMS (Cu)--from water-salt solutions were studied. It was determined difference in peculiarities of proteins sorption depending on its amino acids composition, chemistry of sorbent surface and acidity of medium. It was showed, that modified by cooper (II) sorbent have high affinity to tripsin than albumin in studied solutions. Influence of bearer modification degree on albumin immobilisation and interaction character of SG-PMS (Cu) active centres with function groups of enzyme and albumin have been showed.