Further characterization of the subunits of the giant extracellular hemoglobin of Glossoscolex paulistus (HbGp) by SDS-PAGE electrophoresis and MALDI-TOF-MS

► Monomeric chains c, from the trimer abc reduction, have four isoforms with MM in the range 17,336-17,620 Da. ► Two isoforms, T1 and T2, with MM 51,200 and 51985 Da, are observed for the trimer abc subunit. ► Based on SDS-PAGE, the linker chains L have a high affinity for the trimer abc, appearing on fractions I-V. ► The strong interaction between the linkers and trimer abc makes it difficult the purification of these subunits. ► Monomer d fraction VI appears to be very pure, in agreement with previous studies.