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Deamidations in recombinant human phenylalanine hydroxylase. Identification of labile asparagine residues and functional characterization of Asn --> Asp mutant forms.
Carvalho RN, Solstad T, Bjørgo E, Barroso JF, Flatmark T. Carvalho RN, et al. Among authors: solstad t. J Biol Chem. 2003 Apr 25;278(17):15142-52. doi: 10.1074/jbc.M212180200. Epub 2003 Jan 28. J Biol Chem. 2003. PMID: 12554741 Free article.
Asn(32) in the regulatory domain deamidates very rapidly because of its nearest neighbor amino acid Gly(33) (Solstad, T., Carvalho, R. N., Andersen, O. A., Waidelich, D., and Flatmark, T. (2003) Eur. ...
Asn(32) in the regulatory domain deamidates very rapidly because of its nearest neighbor amino acid Gly(33) (Solstad, T., Carv …
Deamidation of labile asparagine residues in the autoregulatory sequence of human phenylalanine hydroxylase.
Solstad T, Carvalho RN, Andersen OA, Waidelich D, Flatmark T. Solstad T, et al. Eur J Biochem. 2003 Mar;270(5):929-38. doi: 10.1046/j.1432-1033.2003.03455.x. Eur J Biochem. 2003. PMID: 12603326 Free article.
Two dimensional electrophoresis has revealed a microheterogeneity in the recombinant human phenylalanine hydroxylase (hPAH) protomer, that is the result of spontaneous nonenzymatic deamidations of labile asparagine (Asn) residues [Solstad, T. and Flatmark, T. …
Two dimensional electrophoresis has revealed a microheterogeneity in the recombinant human phenylalanine hydroxylase (hPAH) protomer, that i …
57 results