Current developments in chemical cleavage of proteins

Han, Kia‐Ki; Richard, Claude; Biserte, G

doi:10.1016/0020-711x(83)90162-3

Cited by 46 publications

(22 citation statements)

References 35 publications

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“…There, a pronounced decrease (1 Yortho ) or almost complete disappearance (1 Ypara , 1 Ymeta ) was observed, which could indicate further oxidation to occur. Assuming that the oxidative damage observed results from 'moderate' oxidations, peptide cleavage should not result from oxidation (Stadtman 1993), but rather from hydrolysis at labile peptide bonds (Han et al 1983;Kahne and Still 1988). Thus, peptide cleavage would occur independently from the radical-providing sugar moiety, which explains the fact that peptide fragments, but not the tyrosine-containing peptides were produced in significant amounts in the control incubations (Fig.…”

Section: Discussionmentioning

confidence: 93%

Oxidative degradation of N ε-fructosylamine-substituted peptides in heated aqueous systems

2015

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Glycation, or non-enzymatic glycosylation, is a common protein modification formed by reactions between reducing sugars (i.e. aldoses and ketoses) with protein amino groups. Resulting Amadori and Heyns compounds, respectively, can be oxidatively degraded yielding a structurally heterogeneous group of advanced glycation end-products. We have studied this process in aqueous conditions at 95 °C in terms of appearing products and their formation kinetics in the presence or absence of reactive oxygen species (ROS)-generating systems (iron(II) sulfate). RP-HPLC-ESI-MS revealed 20 products, 12 of which were confirmed after synthesis by identical retention times and fragmentation patterns. These products accumulated during the incubation period of 4 h (N(ε)-carboxymethyl-, N(ε)-formyl- and N(ε)-methyl lysine) or appeared intermediately (2-aminoadipic semialdehyde, N(ε)-ethanalyl lysine). Acidic and basic amino acid residues near the glycation site and elevated ROS levels in the reaction mixture had significant effects on both product formation and degradation kinetics.

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Section: Discussionmentioning

confidence: 93%

Oxidative degradation of N ε-fructosylamine-substituted peptides in heated aqueous systems

2015

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“…B ) Recently, Han et al 9 ) have reported that aspartic acid was released from proteins containing aspartyl or asparaginyl residues at a rate at least 100 times faster than any other residue under the same dilute acid treatment described above. Therefore, the amounts of ammonia and aspartic acid released from a soy protein • , ammonia; 0, aspartic acid.…”

Section: Structural Changes Of Soy Protein During Mild Acid Treatmentmentioning

confidence: 93%

Conformational Changes and Functional Properties of Acid-modified Soy Protein

Matsudomi¹,

Sasaki²,

Kato³

et al. 1985

Agricultural and Biological Chemistry

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“…Peptide bonds on either side of aspartic acid are most easily cleaved by acid hydrolysis (Han, Richard, and Biserte 1983). Serine and threonine residues at the N-terminal side are cleaved faster than other amino acid residues.…”

Section: Hydrolysismentioning

confidence: 99%