Reagents for protection of peptide/proteins carbamylation in...

Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai

Reexamination Certificate

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C424S001690

Reexamination Certificate

active

07459425

ABSTRACT:
The present invention generally relates to non-ethylene diamine like compounds that prevent and/or delay carbamylation of peptides.

REFERENCES:
patent: 4605513 (1986-08-01), DiMarchi
patent: 2003/0045004 (2003-03-01), Barri et al.
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Lewis et al. Bendazac prevents cyanate binding to soluble lens proteins and cyanate-induced phase-separation opacities in vitro:a poss. mechanism by which bendazac could delay cataract. Exp. Eye Res.vol. 43 (1986) , pp. 973-979 (In PCT/US2004/00537).
Crompton et al. Aspirin prevents carbamylation of soluble lens proteins and prevents cyanate-induced phase separation opacities in vitro:a poss. mechan. by which aspirin could prevent cataract. Exp. Eye Res.vol. 40 (1985),pp. 297-311 (In PCT/US2004/00537).
International Search Report, No. PCT/US2004/005374, Nov. 22, 2004.
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Lippincott et al., “Carbamylation of Cysteine: A Potential Artifact in Peptide Mapping of Hemoglobins in the Presence of Urea,” Analytical Biochemistry, vol. 267, pp. 57-64 (1999).
Marier et. al., “Determination of Cyanate, and a Study of its Accumulation in Aqueous Solutions of Urea,”Anal. Biochem 7(1964) 304-314.
Stark, G.R., “Modification of Proteins with Cyanate,”Method In Enzymology 11(1967) 590-594.
Stark et. al., “Reactions of the Cyanate Present in Aqueous Urea with Amino Acids and Proteins,”J. Biol. Chem. 235(1960) 3177-3181.
Crompton et al., “Aspirin Prevents Carbamylation of Soluble Lens Proteins and Prevents Cyanate-induced Phase Separation Opacities In Vitro: A Possible Mechanism by which Aspirin could Prevent Cataract,”Exp. Eye Res. 40(1985) 297-311.

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