Primary structure of Vicia angustifolia proteinase inhibitor
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چکیده
منابع مشابه
Primary structure of potato kunitz-type serine proteinase inhibitor.
The serine proteinase inhibitor (PSPI-21) isolated from potato tubers (Solanum tuberosum L.) comprises two protein species with pI 5.2 and 6.3, denoted as PSPI-21-5.2 and PSPI-21-6.3, respectively. They were separated by anion exchange chromatography on a Mono Q FPLC column. Both species tightly inhibit human leukocyte elastase, whereas their interaction with trypsin and chymotrypsin is substan...
متن کاملPrimary structure of a proteinase inhibitor II gene from potato (Solanum tuberosum).
The isolation and characterization of a genomic clone encoding proteinase inhibitor II of potato (Solanum tuberosum) is described. The structure of this gene was determined by sequencing a genomic fragment of about 2 kb containing the entire RNA coding as well as about 900 nucleotides of the 5'-upstream and 250 nucleotides of the 3'-downstream region. The transcription start site was determined...
متن کاملThe proteinase: mucus proteinase inhibitor binding stoichiometry.
In the nanomolar enzyme and inhibitor concentration range, 1 mol of mucus proteinase inhibitor (MPI) inhibits 1 mol of neutrophil elastase, cathepsin G, trypsin, and chymotrypsin. In the micromolar concentration range, the enzyme:inhibitor binding stoichiometry is still 1:1 for elastase but shifts to 2:1 for the three other proteinases. These data could be confirmed by three nonenzymatic method...
متن کاملThe primary structure of Aspergillus niger acid proteinase A.
The complete amino acid sequence of the acid proteinase A, a non-pepsin type acid proteinase from the fungus Aspergillus niger var. macrosporus, was determined by protein sequencing. The enzyme was first dissociated at pH 8.5 into a light (L) chain and a heavy (H) chain, and the L chain was sequenced completely. Further sequencing was performed with the reduced and pyridylethylated or aminoethy...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1984
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1984.tb08421.x