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- W1994240942 abstract "The soy bean trypsin inhibitor of Kunitz contains two tyrosine groups which are susceptible to nitration with tetranitromethane. One of these is in proximity to the critical peptide bond involved in interaction with trypsin. By reduction to aminotyrosine, followed by reaction with dansyl chloride, dansyl substitution may be made at these two sites. The fluorescence properties of the two dansylaminotyrosine groups respond differently to reaction with trypsin and to Kl quenching. A pronounced time dependence of emission spectrum is observed. Ionization of the aminotyrosine group results in a partial quenching of fluorescence, a spectral shift, and a loss of time-resolved spectra. Possible explanations are discussed." @default.
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- W1994240942 date "1974-02-01" @default.
- W1994240942 modified "2023-10-14" @default.
- W1994240942 title "Specifically located fluorescent probes: Properties of a fluorescent conjugate of soy bean trypsin inhibitor containing dansylamino-tyrosine groups" @default.
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- W1994240942 doi "https://doi.org/10.1016/0005-2795(74)90422-x" @default.
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