[Spectra of circular dichroism of proteinase inhibitors from corn].
The circular dichroism spectra of trypsin and chymotrypsin inhibitors from corn seeds were investigated. The spatial organization of the inhibitor molecules was shown to be different. The effects of guanidine chloride and temperature on these proteins suggest that the trypsin inhibitor from corn is much more stable towards the denaturating influences than the chymotrypsin inhibitor.
D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D002942:Circular Dichroism; D004355:Drug Stability; D010944:Plants / Q000032:analysis*; D011480:Protease Inhibitors / Q000302:isolation & purification*; D011487:Protein Conformation; D011489:Protein Denaturation; D014361:Trypsin Inhibitors / Q000302:isolation & purification*; D003313:Zea mays / Q000032:analysis
D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D002918:Chymotrypsin
Spektry krugovogo dikhroizma ingibitorov proteinaz iz kukuruzy.