STRUCTURAL ORGANIZATION OF CHIRONOMUS AGILIS AND C. MURATENSIS (DIPTERA, CHIRONOMIDAE) HEMOGLOBINS

Biochemical studies of two chironomids species show that their hemolymph contains curious hemoglobins. It is unusual that haemoglobin has a low molecular weight, 15.9 kDa for monomeric and 31.4 kDa for dimeric forms, and in a condition of disc-electrophoresis, and they are formed up to 12–16 different fractions of hemoglobins. In hemolymph of Chironomus agilis (Shobanov, Djomin 1988) were found octamers, pentamers, tetramers, trimers, dimers, and monomers, which consist of subunits with MW from 9.6 to 15.7 kDa. In Chironomus muratensis (Ryser, Scholl, Wülker 1983) hemolymph were found octamers, hexamers, tetramers, trimers, dimers, and monomers, which formed from subunits with MW from 11 to 15 kDa.