Zobrazeno 1 - 9
of 9
pro vyhledávání: '"E V, Ievleva"'
Publikováno v:
Applied Biochemistry and Microbiology. 49:514-520
Publikováno v:
Chemistry of Natural Compounds. 29:784-787
From dormant seeds of European yellow lupin (Lupinus luteus) and Washington lupin (Lupinus polyphyllus) inhibitors have been isolated that effectively suppress the activity of trypsin and interact nonstochiometrically with chymotrypsin. From their ph
Publikováno v:
Prikladnaia biokhimiia i mikrobiologiia. 42(3)
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). When studied by SDS-PAGE in the presen
Publikováno v:
Prikladnaia biokhimiia i mikrobiologiia. 41(6)
The activity of trypsin-like proteinases and trypsin inhibitors was measured in fruiting bodies of various species of basidial fungi (Basidiomycetes). Fruiting bodies of all fungi contained these enzymes, with the exceptions of polypore (Coriolus ver
Publikováno v:
Prikladnaia biokhimiia i mikrobiologiia. 40(2)
When grown in a medium containing heat-stable potato tuber proteins, the oomycete Phytophthora infestans (Mont.) de Bary produces a set of exoproteinases active at neutral and mildly basic pH values. These extracellular proteinases have been shown by
Publikováno v:
Prikladnaia biokhimiia i mikrobiologiia. 36(5)
A protein that inhibited the proteolytic activity of trypsin was isolated from amaranth leaves (Amaranthus cruentus) by affinity chromatography on trypsin-Sepharose. The inhibition was noncompetitive (with n-nitroanilide-N-alpha-benzoyl-DL-arginine a
Publikováno v:
Prikladnaia biokhimiia i mikrobiologiia. 19(4)
A method of affinity chromatography of the inhibitor of cysteine proteinases from chick egg protein using immobilized ficin has been developed. This method yields a highly active inhibitor in an essentially homogeneous state. The molecular weight of
Publikováno v:
Prikladnaia biokhimiia i mikrobiologiia. 10(3)
Publikováno v:
Prikladnaia biokhimiia i mikrobiologiia. 12(4)
Pancreatic Kallikrein was purified by affinity chromatography on BPTI-Sepharose. Immobilized BPTI was prepared via three stages: a) formation of the BPTI--acetylated trypsin complex; b) coupling of the resultant complex with CNBr-activated Sepharose;