solanum boliviense/protease

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Kunitz-type protease inhibitors group B from Solanum palustre.

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Five Kunitz protease inhibitor group B genes were isolated from the genome of the diploid non-tuber-forming potato species Solanum palustre. Three of five new genes share 99% identity to the published KPI-B genes from various cultivated potato accessions, while others exhibit 96% identity.

Granulosain I, a cysteine protease isolated from ripe fruits of Solanum granuloso-leprosum (Solanaceae).

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A new cysteine peptidase (Granulosain I) was isolated from ripe fruits of Solanum granuloso-leprosum Dunal (Solanaceae) by means of precipitation with organic solvent and cation exchange chromatography. The enzyme showed a single band by SDS-PAGE, its molecular mass was 24,746 Da (MALDI-TOF/MS) and

In vivo inhibition of Helicoverpa armigera gut pro-proteinase activation by non-host plant protease inhibitors.

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We evaluated 22 different host and non-host plant protease inhibitors (PIs) for in vivo inhibition of Helicoverpa armigera gut pro- and proteinases, and their biological activity against the pod borer, H. armigera, the most important pest of agriculture and horticultural crops worldwide. In vitro

Analysis of mRNAs that Accumulate in Response to Low Temperature Identifies a Thiol Protease Gene in Tomato.

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We have studied the induction of gene expression at low temperature by cloning mRNAs that accumulate when unripe tomato (Lycopersicon esculentum) fruit are incubated at 4 degrees C. Two cloned mRNAs, C14 and C17, accumulate relatively rapidly in response to cold treatment, while a third, C19,

Protease activity of enzyme extracts from tamarillo fruit and their specific hydrolysis of bovine caseins.

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The characterisation of a serine protease isolated from tamarillo (Solanum betaceum) fruit and its milk casein hydrolysis activity were investigated. Compared with calf rennet, a crude extract from tamarillo exhibited wider caseinolytic activity on sodium caseinate. The purified protease was named

The multiple functions of plant serine protease inhibitors: defense against herbivores and beyond.

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Plant protease inhibitors (PIs) are a diverse group of proteins which have been intensely investigated due to their potential function in protecting plants against herbivorous insects by inhibiting digestive proteases. Although this mechanism has been well documented for a number of single PIs and

A model of the C14-EPIC complex indicates hotspots for a protease-inhibitor arms race in the oomycete-potato interaction.

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The oomycete pathogen Phytophthora infestans secretes cystatin-like effector proteins (EPICs) that inhibit secreted host proteases during infection. We recently found that the C14 protease is a relevant target of EPICs and that this protease is under diversifying selection in wild potato species

Impact of recombination on polymorphism of genes encoding Kunitz-type protease inhibitors in the genus Solanum.

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BACKGROUND The group of Kunitz-type protease inhibitors (KPI) from potato is encoded by a polymorphic family of multiple allelic and non-allelic genes. The previous explanations of the KPI variability were based on the hypothesis of random mutagenesis as a key factor of KPI

Protein chips for detection of mite allergens using Kunitz-type protease inhibitors.

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Stored-food and house-dust arthropods include many species of mites and beetles that affect human health. For diagnostic tests proteases such as trypsin are utilized as they are indicators of the presence of allergen contaminants in food. We recently characterized Kunitz-type protease inhibitors

Protease inhibitors and carcinoma of the esophagus.

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BACKGROUND Squamous cell carcinoma of the esophagus is endemic in parts of South Africa. Previous case-control studies have shown many associations but no clear etiologic pathway has been established. METHODS A case-control study of dietary and social factors was performed for 130 patient/control

Purification and characterisation of a protease (tamarillin) from tamarillo fruit.

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A protease from tamarillo fruit (Cyphomandra betacea Cav.) was purified by ammonium sulphate precipitation and diethylaminoethyl-Sepharose chromatography. Protease activity was determined on selected peak fractions using a casein substrate. Sodium dodecyl sulphate polyacrylamide gel electrophoresis

An effector-targeted protease contributes to defense against Phytophthora infestans and is under diversifying selection in natural hosts.

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Since the leaf apoplast is a primary habitat for many plant pathogens, apoplastic proteins are potent, ancient targets for apoplastic effectors secreted by plant pathogens. So far, however, only a few apoplastic effector targets have been identified and characterized. Here, we discovered that the

A role in immunity for Arabidopsis cysteine protease RD21, the ortholog of the tomato immune protease C14.

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Secreted papain-like Cys proteases are important players in plant immunity. We previously reported that the C14 protease of tomato is targeted by cystatin-like EPIC proteins that are secreted by the oomycete pathogen Phytophthora infestans (Pinf) during infection. C14 has been under diversifying

Serine protease inhibitors specifically defend Solanum nigrum against generalist herbivores but do not influence plant growth and development.

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Solanaceaeous taxa produce diverse peptide serine proteinase inhibitors (SPIs), known antidigestive defenses that might also control endogenous plant proteases. If and how a plant coordinates and combines its different SPIs for the defense against herbivores and if these SPIs simultaneously serve

Characterization of a Kunitz-type serine protease inhibitor from Solanum tuberosum having lectin activity.

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Plant lectins and protease inhibitors constitute a class of proteins which plays a crucial role in plant defense. In our continuing investigations on lectins from plants, we have isolated, purified and characterized a protein of about 20 kDa, named PotHg, showing hemagglutination activity from

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