Title: Purification, properties and N-terminal amino acid sequence of a wheat gluten aspartic proteinase
Authors: Bleukx, W ×
Torrekens, S
Van Leuven, Freddy
Delcour, Jan #
Issue Date: Nov-1998
Series Title: Journal of Cereal Science vol:28 issue:3 pages:223-232
Abstract: An aspartic proteinase (EC 3.4.23) was purified 31 300-fold with 6% recovery from wheat gluten by ammonium sulphate precipitation, affinity-chromatography on pepstatin A-agarose and gel permeation chromatography. The enzyme has no amino- or carboxypeptidase activity and is a heterodimer with subunits of apparent molecular mass. c. 11 and 29 kDa. It has an iso-electric point of c. 4.55. The enzyme is maximally active against haemoglobin at pH 2.5 and between 45-50 degrees C and is completely inhibited by pepstatin A. The sequence of the first 20 N-terminal amino acids of the 11 and 29 kDa subunits have 90% and 95% identity, respectively, with the N-terminal amino acid sequences of the 11 and 29 kDa subunits of barley aspartic proteinase. (C) 1998 Academic Press.
ISSN: 0733-5210
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Associated Laboratories - miscellaneous (-)
Centre for Food and Microbial Technology
Department of Human Genetics - miscellaneous
× corresponding author
# (joint) last author

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