Peptide A-glycanases

Suzuki, T., Park, H., Kitajima, K., and Lennarz, W. J. (1998). Peptides glycosylated in the endoplasmic reticulum of yeast are subsequently deglycosylated by a soluble peptide A-glycanase activity. J. Biol. Chem. 273, 21526-21530. 

Suzuki T, Seko A, Kitajima K, Inoue Y, Inoue S (1994) Purification and enzymatic properties of peptide N-glycanase from C3H mouse-derived L-929 fibroblast cells Possible widespread occurrence of post-translational remodification of proteins by N-deglycosylation. J Biol Chem 269 17611-17618 Swaminathan S, Amerik AY, Hochstrasser M (1999) The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast. Mol Biol Cell 10 2583-2594 Tanaka K, Yoshimura T, Tamura T, Fujiwara T, Kumatori A, Ichihara A (1990) Possible mechanism of nuclear translocation of proteasomes. FEBS Lett 271 41-46... 

A.L. Tarentino, C.M. Gomez and T.H. Plummer, Deglycosylation of asparagine-linked gly-cans by peptide iV-glycanase F. Biochemistry, 1985, 24, 4665-4671. 

The development of the continuous-flow FAB interface by Caprioli et al. [8] was primarily directed at the analysis of peptides (Ch. 4.6). Continuous-flow FAB provided reduced suppression of hydrophilic peptides in peptide mixtures. It was widely applied in the field of peptide characterization and the analysis of proteolytic digests, e.g., in the analysis of a tryptic digest of bovine ribonuclease B before and after treatment with N-glycanase [9]. A single injection of 100 pmol provided ca. 70% sequence coverage. 

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