Structural difference of chymotrypsinogens forming chymotrypsin variants in Japanese quail.
A chymotrypsinogen showing the phenotype AA of chymotrypsin was purified from quail pancreas, and its chromatographic behavior, molecular weight, and electrophoretic mobility were very similar to those of another chymotrypsinogen, showing the aa phenotype of chymotrypsin. However, after activation, this chymotrypsinogen from AA showed band 5 of chymotrypsin, while the other chymotrypsinogen from aa did not. Peptide mapping demonstrated that the molecular structures of the two chymotrypsinogens are different. It was recognized that chymotrypsin variants result from activated products of different molecular structures of chymotrypsinogens.
Hou
D X
DX
Department of Animal Science, Faculty of Agriculture, Kagoshima University, Japan.
Maeda
Y
Y
Okamoto
S
S
Hashiguchi
T
T
D000818:Animals; D002845:Chromatography; D002918:Chymotrypsin; D002919:Chymotrypsinogen / Q000032:analysis / Q000737:chemistry* / Q000235:genetics; D003370:Coturnix / Q000235:genetics; D014644:Genetic Variation; D007527:Isoenzymes; D015394:Molecular Structure; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology; D010449:Peptide Mapping; D014357:Trypsin
D007527:Isoenzymes; D002919:Chymotrypsinogen; D002918:Chymotrypsin; D014357:Trypsin