Purification, characterization, protein association property of a non-muscular actin from porcine lung

Global pork production was 101 million tons in 2020. Consequently, a large amount of the porcine viscera were produced simultaneously, of which porcine lung is one major component, so the utilization of these residual materials has garnered significant attention in recent times. In this work, a non-muscular actin (APL) was successfully isolated and purified to homogeneity from porcine lung tissue using a straightforward and efficient protocol. Approximately 100 mg of the protein was obtained from 1 kg of porcine lung tissue. The experimental results showed that the native APL exhibits an apparent molecular mass of about 42 kDa. The amino acid composition analysis demonstrated the presence of all eight essential amino acids in APL. More importantly, APL is rich in magnesium and calcium ions (approximately 33 magnesium ions and 18 calcium ions per molecule). These two metal ions have a great effect on the structure and function of APL. As far as we are aware, this work provides the first systematic report on the purification and characterization of non-muscular actin from porcine lung which represents a newly potential class of magnesium and calcium supplement.