[Secretion of proteolytic enzymes by three phytopathogenic microorganisms].

Serine proteinases from three phytopathogenic microorganisms that belong to different fungal families and cause diseases in potatoes were studied and characterized. The oomycete Phytophthora infestans (Mont.) de Bary and the fungi Rhizoctonia solani and Fusarium culmorum were shown to secrete serine proteinases.

Structure and properties of the potato chymotrypsin inhibitor.

The potato tubers contain proteins that inhibit serine proteinases and belong to subfamily of potato Kunitz-type proteinase inhibitors (PKPI). New highly purified protein had been isolated from mature potato tubers (Solanum tuberosum L., cv.

[Fragment of the gene encoding chymotrypsin and trypsin inhibitor protein of potato tubers].

Product of polymerase chain reaction designated as PKPIJ-B was isolated after amplification from genomic DNA of potato (Solarium tuberosum L., Zhukov Jubilee cultivar) using the designed primers. Nucleotide sequence of PKPIJ-B was determined and amino acid sequence of protein was restored.

[Chymotrypsin and trypsin inhibitor isolated from potato tubers].

Potato Kunitz-type chymotrypsin inhibitor (PKCI-23) was isolated from potato tubers (Solanum tuberosum L., Zhukov's Jubilee breed) and purified to a homogenous state. The protein was purified by gel-filtration chromatography and ion-exchange chromatography using Sephadex G-75 and CM-Sepharose CL-6B, respectively.

Comparative analyses of exoproteinases produced by three phytopathogenic microorganisms.

Proteinases secreted by the oomycete Phytophthora infestans (Mont.) de Bary, Rhizoctonia solani, and Fusarium culmorum belonging to different families of fungi have been studied to determine if the exoenzyme secretion depends on the environmental conditions and the phylogenetic position of the pathogen. The substrate specificity of the extracellular proteinases of F.

Protein trypsin inhibitor from potato tubers.

A protein of 22 kDa designated as PKTI-22 was isolated from potato tubers (Solanum tuberosum L., cv. Istrinskii) and purified to homogeneity using CM-Sepharose CL-6B ion-exchange chromatography.

[Wound healing and induced resistance in potato tubers].

It was demonstrated that biogenic elicitors, arachidonic acid and chitosan, locally and systemically stimulated wound healing in potato tuber tissues by increasing the number of wound periderm layers, accelerating the development of cork cambium (phellogen), and inducing proteinase inhibitors. The signal molecules, jasmonic and salicylic acids, had different effects on the development of wound periderm: jasmonic acid locally and systemically stimulated potato wound healing and elevated the level of proteinase inhibitors, whereas salicylic acid did not have any effect on wound healing and even blocked the formation of proteinase inhibitors.

[Molecular cloning and expression of genes of Kunitz-type C protease inhibitors from potato].

We cloned the products of polymerase chain reaction of the genome DNA of potato (Solanum tuberosum L., Istrinskii cultivar) and isolated 35 clones, which represent copies of eight genes encoding Kunitz type C proteases. Their nucleotide sequences were established.

[Effect of proteinaceous proteinase inhibitors from potato tubers on the growth and development of phytopathogenic microorganisms].

We studied the effect of two proteins, PSPI-21 and PKSI, on the growth and development of phytopathogenic microorganisms (Phytophthora infestans oomycete and Fusarium culmorum fungus). Both proteins were isolated from potato tubers (Solanum tuberosum L., cv.

[Protein inhibitors of fibrin stabilizing factor FXIII].

The ability of cysteine proteinase inhibitors (CPIs) isolated from tubers of potato (Solanum tuberosum) to suppress transpeptidase activity of fibrin stabilizing factor (FXIIIa) through the direct effect on the essential SH group of the enzyme active site has been studied. The formation of fibrin clots soluble in 5 M urea and 2% acetic acid as well as spectrophotometric turbidity analysis of the stabilization and resistance of fibrin clots formed in the presence of FXIIIa and CPIs from potato tubers to plasmin, and electrophoresis of reduced fibrin samples indicate the decrease or absence of covalent crosslinking of fibrin chains. In addition, CPIs added to the substrate proved to decelerate fibrinogen polymerization almost twice relative to control.

Heterologous expression, purification, and properties of a potato protein inhibitor of serine proteinases.

The gene PKPI-B10 [AF536175] encoding in potato (Solanum tuberosum L., cv. Istrinskii) a Kunitz-type protein inhibitor of proteinases (PKPI) has been cloned into the pET23a vector and then expressed in Escherichia coli.

[Interaction between proteinases secreted by the fungal plant pathogen Rhizoctonia solani and natural proteinase inhibitors produced by plants].

The fungal plant pathogen Rhizoctonia solani Kuhn. grown in a medium containing thermostable potato tuber proteins produced proteinases active at moderately alkaline pH values. Electrophoretic analysis in polyacrylamide gel with SDS and copolymerized gelatin showed that the extracellular proteinase complex contained four components that differed in molecular weight.

[Extracellular proteinases from the phytopathogenic fungus Fusarium culmorum].

The growth of Fusarium culmorum fungus on a medium containing thermostable proteins from potato tubers was accompanied by the production of proteinases, exhibiting activity over a broad pH range (from 6.0-10.0).

Subtilisin protein inhibitor from potato tubers.

A protein with molecular weight of 21 kD denoted as PKSI has been isolated from potato tubers (Solanum tuberosum L., cv. Istrinskii).

[Role of proteinase inhibitors in potato protection].

Mechanical damage or infection of potatoes with Phytophthora infestans caused an accumulation of only serine protease inhibitors in exudates of potato tubers. Among them, proteins prevailed that are structurally similar to those present in healthy tubers: a 22-kDa trypsin inhibitor, a 21-kDa serine protease inhibitor consisting of two polypeptide chains, and a 8-kDa potato chymotrypsin I inhibitor produced de novo. The accumulated proteins inhibited the growth of hyphae and germination of zoospores of P.

[Effect of elicitors on accumulation of protease inhibitors in injured potato tubers].

The time course of accumulation and the composition of proteinase-inhibiting proteins in diffusates from potato tubers treated with elicitors such as salicylic, jasmonic, and arachidonic acids were studied. The 40-kDa reserve protein patatin and the chymotrypsin inhibitors, among which proteins of 24.6, 22.

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.

Primary structure of a 21-kD protein from potato tubers.

A 21-kD protein isolated earlier from potato tubers (Solanum tuberosum L.) has two isoforms, with pI 6.3 and 5.

Reactive sites of the 21-kD protein inhibitor of serine proteinases from potato tubers.

The effect of modifications of Met, Arg, and Lys residues on the inhibitory activity of a serine proteinase-inhibiting 21-kD protein from potato tubers has been studied. The data indicate that the 21-kD protein has two independent reactive sites for human leukocyte elastase (or chymotrypsin) and trypsin. It is concluded that the 21-kD inhibitor has Met and Arg residues in the P1 position of the reactive sites responsible for interactions with elastase (or chymotrypsin) and trypsin.

Kunitz-type proteinase inhibitors from intact and Phytophthora-infected potato tubers.

Three protein proteolytic enzyme inhibitors with molecular masses 21, 22, and 23 kDa have been isolated from intact potato tubers (Solanum tuberosum L. cv. Istrinskii).

Potato tuber protein proteinase inhibitors belonging to the Kunitz soybean inhibitor family.

Three protein inhibitors of proteolytic enzymes with molecular weights 21, 22, and 23 kD were isolated from potato tubers (Solanum tuberosum L.) by ammonium sulfate precipitation followed by gel and ion-exchange chromatography. The 21- and 22-kD proteins were shown to be serine proteinase inhibitors with different specificities.

[Isolation and characteristics of a new trypsin and chymotrypsin inhibitor from potato tubers].

A novel trypsin and chymotrypsin inhibitor has been isolated from potato (Solanum tuberosum L.) tubers. The isolation procedure included ammonium sulfate precipitation, gel-chromatography on Sephadex G-75 and ion-exchange chromatography on DEAE-cellulose.