Application of the Lossen Rearrangement of Dinitrophenylhydroxamates to Analysis of Carboxyl Groups in Model Compounds and Gelatin

Gallop, Paul M.; Seifter, Sam; Lukin, Marvin; Meilman, Edward

doi:10.1016/s0021-9258(19)76925-7

Cited by 52 publications

(15 citation statements)

References 26 publications

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“…Although cleavage of cyclic imides by hydroxylamine has not been reported in detail before, the possibility of such cleavage is supported by the observations of Gallop et al (1960). It was found that reaction of polyanhydroaspartic acid with hydroxylamine, under conditions very similar to those used in this work, resulted in extensive degradation of the polymer.…”

Section: Discussionsupporting

confidence: 72%

Structure of α1-CB8, a large cyanogen bromide produced fragment from the α1 chain of rat collagen. The nature of a hydroxylamine-sensitive bond and composition of tryptic peptides

Börnstein¹

1970

Biochemistry

143

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Section: Discussionsupporting

confidence: 72%

Structure of α1-CB8, a large cyanogen bromide produced fragment from the α1 chain of rat collagen. The nature of a hydroxylamine-sensitive bond and composition of tryptic peptides

Börnstein¹

1970

Biochemistry

143

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“…Among the three derivatives (glycine ethyl ester, hydroxylamine, and hydrazine) of fibrin, the fibrin hydroxamate seems best suited for a direct approach. As in the case with gelatin (Gallop et al, 1960), a Lossen rearrangement of the dinitrophenylated fibrin hydroxamate reveals the nature of the acceptor carbonyl functions. Both 7 and (3 carbonyl groups of glutamine and asparagine were shown to be involved (Lorand and Ong, 1966).…”

Section: Resultsmentioning

confidence: 81%

Labeling of Amine-Acceptor Cross-Linking Sites of Fibrin by Transpeptidation^*

Lóránd¹,

Hh²

1966

Biochemistry

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“…-U--Uin peaks IV and VI may be an ester and an amide derivative of ethanolamine, respectively. Incubation of peak IV in 1 M NH2OH at pH 7 and room temperature for 24 h (Gallop et al, 1960) did not remove an ethanolamine moiety from this derivative but led to the formation of peak VI (ca. 30%), indicating that an O -» N acyl migration is faster than hydroxylaminolysis of this ester derivative.…”

Section: Resultsmentioning

confidence: 99%

Modification of catalytic groups in lysozyme with ethylenimine

Yamada¹,

Imoto²,

Noshita³

1982

Biochemistry

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The reaction of lysozyme with ethylenimine has been studied at neutral and acidic pH. At least four singly modified lysozyme derivatives have been isolated. From the product analyses, only carboxyl groups in the protein were found to react. One of the derivatives, 1, was very labile and reverted back to native lysozyme during the isolation procedure. Its formation was markedly inhibited by the presence of tri(N-acetyl-D-glucosamine), indicating that the modified carboxyl residue in 1 is at or close to the binding site of lysozyme for the trisaccharide. Two other derivatives were identified as 2-aminoethyl esters of Glu-35 (2) and Asp-52 (3). At pH 10 and room temperature, these derivatives rearranged to the corresponding 2-hydroxyethylamide derivatives (5 and 6). A fourth derivative (4) did not contain an ethanolamine moiety; nevertheless, its Glu-35 was found to be modified by sequence analysis. Lysozyme derivatives modified at Glu-35 and Asp-52 were inactive toward glycol chitin but retained high affinity for tri(N-acetyl-D-glucosamine). Thus, Glu-35 and Asp-52 are essential for enzyme activity. A mechanism for the selective modification of these carboxyl residues in lysozyme has been proposed and related to the metal binding ability of lysozyme.

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Application of the Lossen Rearrangement of Dinitrophenylhydroxamates to Analysis of Carboxyl Groups in Model Compounds and Gelatin

Cited by 52 publications

References 26 publications

Structure of α1-CB8, a large cyanogen bromide produced fragment from the α1 chain of rat collagen. The nature of a hydroxylamine-sensitive bond and composition of tryptic peptides

Structure of α1-CB8, a large cyanogen bromide produced fragment from the α1 chain of rat collagen. The nature of a hydroxylamine-sensitive bond and composition of tryptic peptides

Labeling of Amine-Acceptor Cross-Linking Sites of Fibrin by Transpeptidation^*

Modification of catalytic groups in lysozyme with ethylenimine

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Application of the Lossen Rearrangement of Dinitrophenylhydroxamates to Analysis of Carboxyl Groups in Model Compounds and Gelatin

Cited by 52 publications

References 26 publications

Structure of α1-CB8, a large cyanogen bromide produced fragment from the α1 chain of rat collagen. The nature of a hydroxylamine-sensitive bond and composition of tryptic peptides

Structure of α1-CB8, a large cyanogen bromide produced fragment from the α1 chain of rat collagen. The nature of a hydroxylamine-sensitive bond and composition of tryptic peptides

Labeling of Amine-Acceptor Cross-Linking Sites of Fibrin by Transpeptidation*

Modification of catalytic groups in lysozyme with ethylenimine

Contact Info

Product

Resources

About

Labeling of Amine-Acceptor Cross-Linking Sites of Fibrin by Transpeptidation^*