Enzyme-inhibitor interactions studied via fluorine nuclear magnetic resonance. I. The interaction of α-chymotrypsin with DL-N-trifluoroacetylphenylalanine
作者： Eugene Zeffren , Roger E. Reavill
DOI: 10.1016/0006-291X(68)90428-2
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摘要: Abstract Fluorine (F 19 ) magnetic resonance has been used to examine the interaction of α-chymotrypsin and DL-N-Trifluoroacetylphenylalanine. The results show that F chemical shift TFAP at pH 6.0 is moved downfield by addition enzyme, while it upfield when compound placed in organic solvents ethanol, dioxane benzene. In absence enzyme NaCl causes a peak, magnitude salt induced directly proportional concentration. may be interpreted either an anisotropic effect or “polar environment before acylation” hypothesis.
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