Abstract
Native glycinin was split by trypsin in limited regions under high ionic strength con-dition and converted into glycinin-T. Initially, the intermediary subunits of glycinin con-verted into fragments of 48, 000 (IST-1) and 44, 500 (IST-2) molecular weights. These frag-ments were transitory intermediates and then they were cleaved yielding fragments of 32, 500 (IST-3) and 29, 000 (IST-4) molecular weights. Analyses of the mole fractions of the frag-ments revealed that IST-2 was rapidly split into IST-4 followed by splitting of IST-1 into IST-3.
Subsequently, glycinin-T was dissociated with 6M urea and subjected to gel filtration and ion exchange chromatography in order to isolate IST-3 and IST-4. Acidic-urea gel electrophoresis of the isolated IST showed that IST-3 contained B1, B2 and B3 subunits, whereas IST-4 contained B4 subunit. These results indicated that IST-3 was formed from IS-I and IS-2, and IST-4 from IS-3.
