Purification and characterization of chymotrypsinogen from pancreas of Japanese quail (Coturnix coturnix japonica).
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. Quail chymotrypsinogen had a mol. wt of 26,100 calculated from amino acid composition data, an isoelectric point of 7.68, a Km of 3.1 mM and K0 of 40.7 sec-1 for tyrosine ester substrate. 3. The activated chymotrypsinogen of quail had a maximum activity at pH 7.0-8.0 and at 45 degrees C, and was stable at pH 4.0-6.0 below 55 degrees C. 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.
Hou
D X
DX
Department of Animal Science, Faculty of Agriculture, Kagoshima University, Japan.
Maeda
Y
Y
Okamoto
S
S
Hashiguchi
T
T
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002845:Chromatography; D002919:Chymotrypsinogen / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D003370:Coturnix / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D007700:Kinetics; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology*; D010449:Peptide Mapping; D014361:Trypsin Inhibitors / Q000494:pharmacology
D000596:Amino Acids; D014361:Trypsin Inhibitors; D002919:Chymotrypsinogen