TY - JOUR
AU - ISHII,, Shin-ichi
AB - Abstract The reactivities of the active-site histidine residue in bovine trypsin and its anhydro-derivative, as well as in Streptomyces griseus trypsin and its anhydro-derivative have been compared. The reactivity with TLCK was found to be lost in both of the anhydrotrypsins. On the other hand, alkylation by iodoacetamide either in the presence or absence of 1-methylguanidine proceeded faster in anhydrotrypsins than in trypsins. These differential responses to alkylating reagents are discussed in terms of a subtle change in the active-site conformation which occurs during the conversion of trypsin into anhydrotrypsin. The examination of difference CD spectra, produced by interaction with benzamidine or β-naphthamidine, also suggested a conformational difference of the active-site between the proteins of bovine origin. This content is only available as a PDF. Author notes 1This work was supported in part by a grant from the Ministry of Education, Science and Culture of Japan. © BY THE JOURNAL OF BIOCHEMISTRY
TI - Anhydrotrypsin and Trypsin: Subtle Difference in the Active-site Conformations Detected by Chemical Modification and CD Spectroscopy
JF - The Journal of Biochemistry
DO - 10.1093/oxfordjournals.jbchem.a131501
DA - 1977-03-01
UR - https://www.deepdyve.com/lp/oxford-university-press/anhydrotrypsin-and-trypsin-subtle-difference-in-the-active-site-Lq02T16t0f
SP - 657
EP - 663
VL - 81
IS - 3
DP - DeepDyve
ER -