Primary Structure of Potato Kunitz-Type Serine Proteinase Inhibitor
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Tatyana A. Valueva
, Tatyana A. Revina , Vladimir V. Mosolov and Reinhard Mentele
Abstract
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 substantially weaker. The sequences of both PSPI-21-5.2 and PSPI-21-6.3 were determined by analysis of overlapping peptides obtained from the oxidized or reduced and S-pyridylethylated proteins after digestion with trypsin or pepsin. Both species of PSPI-21 are composed of two chains, named chains A and B, which are linked by a disulfide bridge between Cys(146) and Cys(157). The other disulfide bridge is located within the A chains between Cys(48) and Cys(97). The amino acid sequences of the large A chains of the two forms, consisting of 150 amino acids residues each, differ in a single residue at position 52. The small chains B, containing 37 and 36 residues in PSPI-21-6.3 and PSPI-21-5.2, respectively, have nine different residues. The entire amino acid sequences of the two inhibitors show a high degree of homology to the other Kunitz-type proteinase inhibitors from plants.
Copyright © 2000 by Walter de Gruyter GmbH & Co. KG
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- Content Index
- Author Index
- Subject Index
Articles in the same Issue
- Circadian Rhythms of Sterol 12α-Hydroxylase, Cholesterol 7α-Hydroxylase and DBP Involved in Rat Cholesterol Catabolism
- Mannosidase Action, Independent of Glucose Trimming, Is Essential for Proteasome-Mediated Degradation of Unassembled Glycosylated Ig Light Chains
- Characterization of a Receptor for Heat Shock Protein 70 on Macrophages and Monocytes
- Yeast Translational Activator Cbs2p: Mitochondrial Targeting and Effect of Overexpression
- Mutational Scanning of a Hairpin Loop in the Tryptophan Synthase β-Subunit Implicated in Allostery and Substrate Channeling
- The Difference in the Carboxy-Terminal Sequence Is Responsible for the Difference in the Activity of Chicken and Rat Liver Fructose-2,6-Bisphosphatase
- Crystal Structure of the Caspase Activator Human Granzyme B, a Proteinase Highly Specific for an Asp-P1 Residue
- Primary Structure of Potato Kunitz-Type Serine Proteinase Inhibitor
- Activation of proPHBSP, the Zymogen of a Plasma Hyaluronan Binding Serine Protease, by an Intermolecular Autocatalytic Mechanism
- Human and Rat Dipeptidyl Peptidase III: Biochemical and Mass Spectrometric Arguments for Similarities and Differences
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- Content Index
- Author Index
- Subject Index