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• W1566208794 abstract "The two-disulfide peptide 62–68 (Cys 64–Cys 80) 74–97 (Cys 76–Cys 94) has been shown in previous reports in this series to carry a full antigenic reactive site of lysozyme. It was also shown that the reactive site required, for appropriate reactivity, one or both of tryptophans 62 and 63 and one or both of lysines 96 and 97. Also, some or all of the region 84–93 around Asp 87 was needed for achievement of full reactivity. When the contribution of the latter was obliterated, the reactivity of the site decreased (from about 28–33% down to 13–16%; Atassi et al., 1976a). The integrity of the disulfides 64–80 and 76–94 was critical for bringing the various regions of the site into close proximity. In the present communication, the independent roles of the two trytophans and the two lysines were investigated by studying the immunochemistry of seven synthetic peptides. These peptides were designed to stimulate the sequences: 62–64 linked to 76–80 which is in turn linked to sequence 94–97. However, we have employed a novel and an unorthodox approach in that our synthetic peptides carried diglycyl segments instead of disulfide bonds. Also, the four peptide bonds in the central part of each synthetic peptide (designed to simulate the segment 76–80) were of the opposite direction to the natural sequence. In several of the peptides, tryptophan residues were substituted by phenylalanine. Peptides with one tryptophan, one phenylalanine or two phenylalanines at the amino end possessed comparable inhibitory activities which approximated the aforementioned expected value. When the peptide did not carry a tryptophan or a phenylalanine at the amino end, the inhibitory activity decreased drastically (down to 3–5%). Removal of one or two lysines on the C-terminal end of the peptides (but adding back two phenylalanines at the amino end to maintain size and contribution of that portion to immunochemical reaction) had an adverse effect on the immunochemical reaction. The decrease in inhibitory activity was greater on deletion of the last lysine than on deletion of the second lysine. These studies showed that only one tryptophan (residue 62) is part of the antigenic site in lysozyme, whereas both lysines are required for the reactivity of the site with one being more critical than the other. The results also indicated that diglycyl segments substituted with surprising" @default.
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• W1566208794 date "1976-08-01" @default.
• W1566208794 modified "2023-09-24" @default.
• W1566208794 title "Enzymic and immunochemical properties of lysozome—XV" @default.
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• W1566208794 doi "https://doi.org/10.1016/0019-2791(76)90209-3" @default.
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