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The amino acid sequence and reactive inhibitory site of the major trypsin isoinhibitor de 5 isolated from seeds of the brazilian carolina tree adenanthera pavonina


Biochimica et Biophysica Acta 872(1-2): 134-140
The amino acid sequence and reactive inhibitory site of the major trypsin isoinhibitor de 5 isolated from seeds of the brazilian carolina tree adenanthera pavonina
Eight iso-inhibitors of trypsin were isolated from seeds of the Brazilian Carolina tree (Adenanthera pavonina L.) by precipitation with ammonium sulphate, gel filtration, affinity chromatography on enzymatically inert anhydrotrypsin Sepharose 4B, and separated by ion-exchange chromatography on DEAE-Sepharose. The pI values of the isoinhibitors (DE1-DE8) ranged from 5.10 to 4.40. Each isoinhibitor had an Mr of approx. 21 000 and was composed of a large .alpha. chain (Mr 16 000) and a smaller .beta. chain (Mr 5000) linked together by a disulphide bond. The complete amino acid sequence of isoinhibitor DE5 (pI 4.75) was deduced by analysis of peptides and fragments derived from the separated .alpha. and .beta. chains by digestion with trypsin, chymotrypsin, pepsin, thermolysin, the Staphylococcus aureus V8 proteinase and iodosobenzoic acid. The sequence of the Carolina DE5 isoihibitor and the location of its reactive (trypsin-inhibitory) peptide bond showed clear homology with the Kunitz-type proteinase inhibitors from soybean, winged bean and a number of other legume seeds.


Accession: 006599161

DOI: 10.1016/0167-4838(86)90156-1



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