Journal Article

Bond-Specific Chemical Cleavages of Peptides and Proteins with Perfluoric Acid Vapors: Novel Peptide Bond Cleavages of Glycyl-Threonine, the Amino Side of Serine Residues and the Carboxyl Side of Aspartic Acid Residues

Takao Kawakami, Masaharu Kamo, Keiji Takamoto, Kenji Miyazaki, Lu-Ping Chow, Yoshio Ueno and Akira Tsugita

in The Journal of Biochemistry

Published on behalf of The Japanese Biochemical Society

Volume 121, issue 1, pages 68-76
Published in print January 1997 | ISSN: 0021-924X
Published online January 1997 | e-ISSN: 1756-2651 | DOI: http://dx.doi.org/10.1093/oxfordjournals.jbchem.a021572
Bond-Specific Chemical Cleavages of Peptides and Proteins with Perfluoric Acid Vapors: Novel Peptide Bond Cleavages of Glycyl-Threonine, the Amino Side of Serine Residues and the Carboxyl Side of Aspartic Acid Residues

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Peptide bond cleavages by vapors composed of various from aqueous solutions of perfluoric acid were studied using synthetic peptides and proteins, and specific conditions were established for peptide bond cleavages including a novel cleavage of the glycyl-threonine bond. The peptide bonds on the aminosides of serine residues were cleaved by exposure to a vapor of 75%aqueous heptafluorobutyric acid at 30 or 50°C for 24 h. Glycyl-threonine peptide bonds were cleaved with vapors of various concentrations (5, 75, and 90%) of heptafluorobutyric acid at 30–40°C for 24 h. The peptide bonds on the carboxylsides of aspartic acid residues were cleaved by exposure to a vapor of 0.2% heptafluorobutyric acid at 90°C for 4 to 24 h. The same vapor cleaved aspartyl-proline bonds under milder conditions such as at 60°C for 16 h, under which the other aspartyl bonds were uncleaved. These specific chemical cleavages were applied to several proteins including newly characterized proteins.

Keywords: Asp-C cleavage; Asp-Pro cleavage; Gly-Thr cleavage; perfluoric acid; Ser-N; cleavage

Journal Article.  0 words. 

Subjects: Biochemistry

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