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vicia angustifolia/proteinase
Veza se sprema u međuspremnik
6 rezultatima
Trypsin reactivity site of the Vicia angustifolia proteinase inhibitor.
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Prijava Registriraj se
Trypsin [EC 3.4.21.4] modified (reactive site cleaved) Vicia angustifolia proteinase inhibitor was prepared at pH 3 with a catalytic amount of trypsin and purified using columns of Sephadex G-50 and DEAE-Sephadex A-25. The modified inhibitor, which still retained antitryptic activity, lost its
Primary structure of Vicia angustifolia proteinase inhibitor.
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Prijava Registriraj se
The complete amino acid sequence (72 amino acid residues) of a double-headed proteinase inhibitor from seeds of Vicia angustifolia L. var. segetalis Koch has been determined and compared with those of other double-headed inhibitors of known structure. Sequencing was performed by conventional methods
Isolation and activities of the trypsin-modified Vicia angustifolia proteinase inhibitor lacking carboxyl-terminal hexapeptide.
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The Vicia angustifolia proteinase inhibitor was incubated with p-toluenesulfonyl-L-phenylalanine chloromethyl ketone-trypsin (EC 3.4.21.4) and a main product was isolated. The purified product was different to the first trypsin-modified V. angustifolia inhibitor. The C-terminal residues of the new
Proteinase inhibitor from Vicia angustifolia L. var. segetalis Koch. Isolation, characterization, and chemical modification.
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The amino acid sequence of a Bowman-Birk type proteinase inhibitor from faba beans (Vicia faba L.).
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Prijava Registriraj se
The amino acid sequence of a Bowman-Birk type proteinase inhibitor (FBI) from seeds of faba bean (Vicia faba L.) was determined by analysis of peptide fragments generated by reduction and S-carboxymethylation of enzymatically modified inhibitors, which were obtained from native FBI by limited
Amino acid sequence of a Bowman-Birk proteinase inhibitor from pea seeds.
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Prijava Registriraj se
Trypsin inhibitors from winter pea seeds (c.v. Frilene) have been purified by ammonium sulfate precipitation, gel filtration, and anion and cation exchange chromatography and shown to consist of six protease inhibitors (PSTI I, II, III, IVa, IVb, and V). Their molecular weights were determined by
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