Abstract
Wheat serpin genes have been identified by Southern blot hybridization with three distinct barley protein Z probes. Immunoblot analysis with a monoclonal antibody towards barley protein Z confirmed expression of related Mr ~ 40 kDa proteins in wheat grain. The wheat serpins were extracted under reducing conditions and separated from β-amylase and other seed proteins by thiophilic adsorption and anion-exchange chromatography. One molecular form possessing chymotrypsin inhibitory activity was isolated in a reactive site cleaved form on a chymotrypsin affinity column. N-terminal amino acid sequences of a CNBr fragment and of the C-terminal peptide from the cleaved inhibitor (Mr 4574 ± 4 Da) verified homology with barley protein Z and mammalian serpins. The native inhibitory serpin was demonstrated to form an SDS-stable complex with α-chymotrypsin.
Original language | English |
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Journal | F E B S Letters |
Volume | 343 |
Issue number | 1 |
Pages (from-to) | 75-80 |
ISSN | 0014-5793 |
DOIs | |
Publication status | Published - 1994 |