Human erythrocyte actin (band 5) was purified by acetone powder extraction, repeated F-G exchange and gel filtration on a Sephadex G-150 column in the presence of sodium dodecyl sulfate (SDS). The molecular weight of the purified erythrocyte actin was determined to be 43, 500 by sedimentation equilibrium. Isoelectric focusing gel analysis showed that the purified erythrocyte actin existed in the β-form with an isoelectric point between those of rabbit skeletal muscle α-actin and chicken gizzard γ-actin. The purified erythrocyte actin was found to be very similar to other actins in amino acid compositions and in the electrophoretic analysis after the CNBr-degradation.
Photoelectric effects are studied in the thin-films of chlorophyll-a and/or chlorophyll-b formed at liquid/liquid interfaces without other surface-active components. The open circuit photovoltages of chlorophyll-a thin-films are greater than that of BLM (bilayer lipid membranes) of widely used chloroplast extracts under the symmetrical 0.1 M KCl solution. Futhermore, the chemical stability of chlorophyll molecules in the film is checked by using both thin-layer chromatography and spectrophotometry.