Elution Profile of Muscular Protein from Antarctic Krill in Sepharose C1-4B Gel Filtratin

Abstract

Muscular protein was freshly extracted with media containing high salt concentrations of I=0.5-1.0 from Antarctic krill Euphausia superba immediately after being caught.
The molecular composition of the extracted protein was roughly discussed by Sepharose C1-4B gel filtration. SDS-gel electrophoretic pattern, viscosity and ATPase activity were also measured to characterize the protein component in the extract.
By gel filtration, the extracted protein with I=0.5 as well as I=1.0 media was separated into three protein fractions: A, b and C in order of molecular size from the large to the small. In addition to SDS-gel electrophoretic patterns of the three fractions, viscosity and ATPase activity of the extracted protein proved that the A and B fractions were composed of actomyosin with different molecular size. A large portion of the C fraction was found to be water soluble protein component which were extractable with medium of I=0.05.
The amout of the components in B fraction decreased with the increase in the component of A fraction during storage for a short period or washing-treatment of muscle.