1983
DOI: 10.1248/cpb.31.1067
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Apparent autolysis of the N-terminal tetrapeptide of vasoactive intestinal polypeptide (VIP).

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“…We reported that the V domains of essentially all Abs contain enzyme-like nucleophiles that form covalent adducts with phosphonate diesters containing a positive charge in the immediate vicinity of the phosphorus [32]. Various non-enzymatic, non-Ab proteins also react covalently with the electrophilic phosphorus [33], and other groups have inferred serine protease-like nucleophiles in peptides and proteins that are not usually classified as enzymes, e.g., glucagon and VIP [34,35]. Interestingly, certain proteins subjected to irreversible heat denaturation displayed increased nucleophilic reactivity [33].…”
Section: Protein Nucleophilic Sitesmentioning
confidence: 99%
“…We reported that the V domains of essentially all Abs contain enzyme-like nucleophiles that form covalent adducts with phosphonate diesters containing a positive charge in the immediate vicinity of the phosphorus [32]. Various non-enzymatic, non-Ab proteins also react covalently with the electrophilic phosphorus [33], and other groups have inferred serine protease-like nucleophiles in peptides and proteins that are not usually classified as enzymes, e.g., glucagon and VIP [34,35]. Interestingly, certain proteins subjected to irreversible heat denaturation displayed increased nucleophilic reactivity [33].…”
Section: Protein Nucleophilic Sitesmentioning
confidence: 99%