Purification and characterization of chymotrypsinogen from pancreas of Japanese quail ( Coturnix coturnix japonica)

Abstract

1. 1. A chymotrypsinogen from pancreas of Japanese quail ( Coturnix coturnix japonica) was purified by acid extraction, salt fractionation and chromatographic separation on CM-cellulose and Sephadex G-100, and gave a single protein band on SDS-PAGE. 2. 2. Quail chymotrypsinogen had a mol. wt of 26, 100 calculated from amino acid composition data, an isoelectric point of 7.68, a K m of 3.1 mM and K 0 of 40.7 sec −1 for tyrosine ester substrate. 3. 3. The activated chymotrypsinogen of quail had a maximum activity at pH 7.0–8.0 and at 45°C, and was stable at pH 4.0–6.0 below 55°C. 4. 4. Comparison of quail and bovine chymotrypsinogens indicates that the activities of the enzymes from quail and bovine are more constant than their physical characteristics.