Broad-Specificity Proteinase Inhibitors in Scopolia japonica (Solanaceae) Cultured Cells. Isolation, Physicochemical Properties, and Inhibition Kinetics
| Autor: | Kuniaki Sakato, Masanaru Misawa, Hozumi Tanaka |
|---|---|
| Rok vydání: | 1975 |
| Předmět: |
Biochemistry
Chromatography Affinity Cell Line chemistry.chemical_compound Affinity chromatography medicine Protease Inhibitors Amino Acids chemistry.chemical_classification Chymotrypsin Chromatography Molecular mass biology Plants Chromatography Ion Exchange Trypsin biology.organism_classification humanities Amino acid Molecular Weight Kinetics Papain Optical Rotatory Dispersion Enzyme chemistry Scopolia japonica biology.protein Peptides medicine.drug |
| Zdroj: | European Journal of Biochemistry. 55:211-219 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1111/j.1432-1033.1975.tb02153.x |
| Popis: | Proteinase inhibitors were isolated from Scopolia japonica cultured cells. Isolation procedures involve concentration by a hydrophobic resin of Diaion HP-20, decolorization by Duolite A-7, affinity chromatography on trypsin-Sepharose, and Bio-Gel P-4 chromatography. It was found that the proteinase inhibitors from S. japonica cells are a mixture of at least five components. For the inhibitory components except one, amino acid analyses, measurements of sedimentation equilibrium and optical rotatory dispersion (ORD) were carried out. The inhibitors were shown to be the polypeptides with molecular weights in the range of approximately 4000 to 6000. In addition, one of them was found to have approximately 15%α-helical conformation by the Moffitt-Yang analysis of ORD data. The inhibitors were found to have potent inhibitory activity for trypsin, chymotrypsin, plasmin, kallikrein and pepsin but not for papain with synthetic and natural substrates. These inhibitors formed stable complexes with trypsin and chymotrypsin in an equimolar ratio, and their inhibitory mechanisms for both enzymes were of non-competitive type. |
| Databáze: | OpenAIRE |
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