Purification, properties and N-terminal amino acid sequence of a wheat gluten aspartic proteinase |
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| Authors: | W Bleukx S Torrekens F Van Leuven JA Delcour |
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| Institution: | aKatholieke Universiteit Leuven, Laboratorium voor Levensmiddelenchemie, Kardinaal Mercierlaan 92, B-3001 Heverlee, Belgium;bKatholieke Universiteit Leuven, Centrum Menselijke Erfelijkheid, Herestraat 49, B-3000 Leuven, Belgium |
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| 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°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. |
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| Keywords: | gluten aspartic proteinase characterisation amino acid sequence |
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