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1.
Prikl Biokhim Mikrobiol ; 44(1): 101-5, 2008.
Article in Russian | MEDLINE | ID: mdl-18491605

ABSTRACT

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. Istrinskii) and served as inhibitors of serine proteinases. These proteins differed in the ability to inhibit growth of Phytophthora infestans oomycete and Fusarium culmorum fungus. PSPI-21 was the most potent in modulating the growth of oomycete mycelium. PKSI primarily affected the growth of the fungal mycelium. The proteins under study induced complete destruction of oomycete zoospores and partial destruction of fungal macroconidia. Our results suggest that these proteins are involved in the protection of potato plants from phytopathogenic microorganisms.


Subject(s)
Fusarium/drug effects , Phytophthora/drug effects , Plant Proteins/pharmacology , Serine Proteinase Inhibitors/pharmacology , Solanum tuberosum/chemistry , Fusarium/growth & development , Intracellular Signaling Peptides and Proteins/pharmacology , Mycelium/drug effects , Mycelium/growth & development , Phosphoproteins/pharmacology , Phytophthora/growth & development , Plant Tubers/chemistry , Serine Proteinase Inhibitors/isolation & purification
2.
Biokhimiia ; 60(11): 1844-52, 1995 Nov.
Article in Russian | MEDLINE | ID: mdl-8590757

ABSTRACT

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. The inhibitor interacts with trypsin and chymotrypsin at a molar ratio of 1:1. The substrate-dependent dissociation of the enzyme-inhibitor complexes is observed. The inhibitor displays no activity towards subtilisin and pancreatic elastase. The ability of the inhibitor to form a ternary complex containing simultaneously both trypsin and chymotrypsin molecules testifies to the presence of two independent reactive sites for these enzymes.


Subject(s)
Chymotrypsin/antagonists & inhibitors , Trypsin Inhibitors/isolation & purification , Amino Acid Sequence , Chromatography, DEAE-Cellulose , Chromatography, Gel , Electrophoresis, Polyacrylamide Gel , Molecular Sequence Data , Substrate Specificity , Trypsin Inhibitors/metabolism
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