Ontology highlight
ABSTRACT:
SUBMITTER: Rydberg EH
PROVIDER: S-EPMC2144294 | biostudies-other | 1999 Mar
REPOSITORIES: biostudies-other
Rydberg E H EH Sidhu G G Vo H C HC Hewitt J J Côte H C HC Wang Y Y Numao S S MacGillivray R T RT Overall C M CM Brayer G D GD Withers S G SG
Protein science : a publication of the Protein Society 19990301 3
Human pancreatic alpha-amylase (HPA) was expressed in the methylotrophic yeast Pichia pastoris and two mutants (D197A and D197N) of a completely conserved active site carboxylic acid were generated. All recombinant proteins were shown by electrospray ionization mass spectrometry (ESI-MS) to be glycosylated and the site of attachment was shown to be Asn461 by peptide mapping in conjunction with ESI-MS. Treatment of these proteins with endoglycosidase F demonstrated that they contained a single N- ...[more]