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under nonbiological conditions, and biochemists who apply these reagents making
the assumption that their mechanisms of action in aqueous biological environments
are well understood. This situation has been succinctly summarized by Russian
workers as follows, “The opinion dominates in the literature that, in the case of
reagents carrying aromatic azide groups, including 5-azido-2-nitrobenzoyl group,
the reactive particles modifying the protein functional groups are aryl nitrenes
formed under irradiation. These conclusions are based on the speculations concern-
ing the results of kinetic studies and the identification of stable products isolated after
the azide photolysis in organic media, i.e., under the conditions far from those used in
the protein affinity modifications”. 153 It is to be hoped that mechanistic chemists will
rectify this situation by extending their studies into aqueous media with biological
molecules and that biological chemists will provide more detailed information about
the structures of the cross-linked products that they isolate from their diverse studies.
With such a synergy of effort, it should be possible to design PAL agents that are
custom designed for a wide variety of molecular situations.
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