phaseolus aconitifolius/protease

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Coordination of protein and mRNA abundances of stromal enzymes and mRNA abundances of the Clp protease subunits during senescence of Phaseolus vulgaris (L.) leaves.

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Our objective was to determine the coordination of transcript and/or protein abundances of stromal enzymes during leaf senescence. First trifolioliate leaves of Phaseolus vulgaris L. plants were sampled beginning at the time of full leaf expansion; at this same time, half of the plants were switched

Resolution of proteases in the keratinolytic larvae of the webbing clothes moth.

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The proteases of the larvae of the webbing clothes moth, Tineola bisselliella, were investigated because of this organism's phylogenetic rank as a member of the lower invertebrates, its unique position as one of the relatively few organisms that can digest keratin and its importance as a serious

Unusual structural characteristics and complete amino acid sequence of a protease inhibitor from Phaseolus acutifolius seeds.

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Two isoforms of a protease inhibitor were isolated by ion-exchange chromatography of tepary bean (Phaseolus acutifolius G.) seed proteins. The main isoform was used to determine the amino acid sequence of the protein. It is an 80 amino acid residue protein with a molecular mass of 8765 Da, showing

Properties of a Non-canonical Complex Formed Between a Tepary Bean (Phaseolus acutifolius) Protease Inhibitor and α-Chymotrypsin.

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Protease inhibitors are crucial for the control of proteolytic activity in different physiological processes. However, some inhibitors do not show canonical enzyme recognition of the enzyme under certain conditions. In this work, we present evidence that indicates the formation of an active complex

Independent heat stabilization of proteases associated with multiheaded inhibitors. Complexes of chymotrypsin, subtilisin and trypsin with chicken ovoinhibitor and with lima bean protease inhibitor.

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The heat stabilization resulting from specific association of serine proteases with either of two multiheaded protease inhibitors, chicken ovoinhibitor or lima bean protease inhibitor, was determined at pH 6.7 in a differential scanning calorimeter. The 2:1 complex of either bovine

Biochemical characterization of extracellular proteases from Vibrio cholerae.

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Isoelectric focusing of culture supernatants from Vibrio cholerae El Tor 1621 and high protease-producing mutant strain 1621 hip revealed the presence of three different types of extracellular protease. Type I protease was the major activity in the wild-type strain and was inhibited by

Characterization of an extracellular matrix-degrading protease derived from a highly metastatic tumor cell line.

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A proteolytic activity associated with the microsomal fraction of L-5178Y/Esb tumor cells has been characterized. The enzyme has a molecular weight of 80-90 kD as determined by affinity-labelling with [3H]DFP and SDS-gel electrophoresis. It cleaves ester substrates at the carboxyl position of lysine

Preparation of protease-free and ribonuclease-free pancreatic deoxyribonuclease.

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When pancreatic DNase I is used as a specific biochemical reagent in the preparation of nuclear ribonucleic acids or nuclear proteins, freedom from contaminating ribonucleases or proteases is an important property of the enzyme preparation. A simple one-step procedure has been developed to effect

A novel alkaline protease from wild edible mushroom Termitomyces albuminosus.

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A protease with a molecular mass of 30 kDa and the N-terminal sequence of GLQTNAPWGLARSS, was isolated from fresh fruiting bodies of the wild edible mushroom Termitomyces albuminosus. The purification protocol included ion exchange chromatography on DEAE-cellulose, Q-Sepharose, SP-Sepharose and

Demonstration of kallikrein-like protease activity in nonactivated plasma of patients with Cooley's anemia.

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Routine evaluation of 12 children with Cooley's anemia revealed that each one had a prolonged partial thromboplastin time. However, prothrombin time and thrombin time were within the normal range. Specific assays demonstrated low levels of the four contact factors: factors XI, XII, prekallikrein,

Role of gastric juice in feedback regulation of rat pancreatic secretion by luminal proteases.

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The role of gastric juice in the intestine on the pancreatic secretory response to intraduodenal infusion of trypsin inhibitors or to diversion of bile and pancreatic juice from the intestine was studied in conscious rats with pylorus ligation and gastric juice drainage. In absence of gastric juice

Activation of rat serosal mast cells by chymase, an endogenous secretory granule protease.

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Chymase, the major neutral protease of the rat serosal mast cell (RMC) secretory granule, causes RMC to release their secretory granules and to oxidatively metabolize endogenous arachidonic acid to prostaglandin D2 (PGD2). The granule markers, endogenous beta-hexosaminidase and exogenously added

Contact factor proteases and the complexes formed with alpha 2-macroglobulin can interfere in protein C assays by cleaving amidolytic substrates.

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Plasma from women taking combined oral contraceptives and cold-activated plasma contain proteases which cleave chromogenic substrates in protein C assays in the absence of protein C activators such as Protac. This spontaneous activity makes a background substraction necessary and makes protein C

Characterization of a membrane protease from rat submaxillary-gland mitochondria that possess thrombin-like activity.

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A membrane protease possessing thrombin-like activity was purified to homogeneity from mitochondria of rat submaxillary gland. The molecular mass of the enzyme was determined to be 45 kDa by SDS/PAGE under reducing conditions and by gel filtration on a Sephadex G-100 column. The enzyme is a

Partial characterization of trypsin-like protease and molecular cloning of a trypsin-like precursor cDNA in salivary glands of Lygus lineolaris.

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Based on substrate specificity, an alkaline pH optimum, sensitivity to selected proteinase inhibitors, and molecular analysis, we provide evidence for the presence of a trypsin-like serine proteinase in the salivary gland complex (SGC) of the tarnished plant bug, Lygus lineolaris (Palisot de

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