PubMed Health⌕ Search

Biomedical subjects

V V Mosolov

Publications and source records attributed to V V Mosolov.

At least 55 records · Page 3Linked to original sources
PubMedDate not supplied

[Purification of pancreatic kallikrein by the method of affinity chromatography].

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; c) dissociation of the bound complex at pH 2.0 to yield immobilized BPTI and acetylated trypsin. The final product contained 59 X 10(-3) micronmoles insolubilized BPTI/ml Sepharose. Trypsin occurring in commercial Kallikrein preparations was separated by the batch procedure with ovomucoid-Sepharose. This method allows 100-fold purification of commercial Kallikrein.

Animals↗
PubMedDate not supplied

[Trypsin inhibitor from Amaranth (Amaranthys cruentus) leaves].

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 as substrate) and had a Ki of 11.87 x 10(-7) 7 M. The protein caused a weaker inhibitory effect on chymotrypsin, had no effect on subtilisin, displayed a molecular weight of 8 kDa, and contained no cysteine residues.

Hydrolysis↗
PubMedDate not supplied

[Plant proteinase inhibitors as polyfunctional proteins (a review)].

Literature data on plant proteinase inhibitors as multifunctional proteins are reviewed. In addition to the direct inhibitory effect on enzymes, these proteins may function in other processes, particularly under biotic and environmental stressful conditions. A special section discusses the relationships of plant proteinase inhibitors and storage proteins.

2S Albumins, Plant↗
PubMedDate not supplied

[Study of thermostable proteins in potatoes by isoelectric focusing].

With the aid of the method of isoelectric focusing eight thermostable proteins with isoelectric points of 3.6, 3.9, 4.u, 5.1, 5.8, 6.6, 7.2 and 10.0 were found in the extract from potato tubers of the Lyubimets variety. All the proteins had inhibitory activity in relation to alpha-chymotrypsin and trypsin.

Chymotrypsin↗
PubMedDate not supplied

[Proteinase inhibitors and their function in plants: a review].

The spread, classifications, and properties of plant proteins capable of inhibiting proteinases have been reviewed. Data from the literature on the likely physiological functions of these inhibitors in plants are analyzed.

Amino Acid Sequence↗
PubMedDate not supplied

[Properties of immobilized trypsin and alpha-chymotrypsin and their use for purification of proteinase inhibitors from potatoes].

Immobilized trypsin and alpha-chymotrypsin were obtained as a result of the enzyme attachment to bromo-cyanogen activated cepharose. Proteolytic activity (substrate--casein) of immobilized trypsin and alpha-chymotrypsin was 18.7 and 9%, respectively and their esterase activity with methyl ester benzoyl-L-arginine (trypsin) and ethyl ester acetyl-L-tyrosine (alpha-chymotrypsin) was 75 and 20% of that of soluble enzymes. Immobilized enzymes were used to purify proteinase inhibitors from potatoes by affine chromatography. Specific activity of trypsin and chymotrypsin inhibitors was increased 10 and 6 times, respectively. By isoelectric focussing it was shown that the purified preparation of chymotrypsin inhibitors consisted of two acid proteins and one alkaline protein, the latter being in predominance. The purified preparation of trypsin inhibitors contained equal amounts of proteins with the isoelectric point at pH 7.1 and 8.9 and a low quantity of the component with the isoelectric point at pH 5.7.

Binding Sites↗
PubMedDate not supplied

[Protease inhibitors in plants].

Physico-chemical properties, primary structure and mechanism of action of proteins--proteinase inhibitors from plant sources are reviewed. The perspectives of their application in medicine are discussed.

Amino Acid Sequence↗
PubMedDate not supplied

[Biospecific sorbent for removal of proteinases from biological fluids].

Sorbents for removal of proteases from biological fluids were synthesized via immobilization of a specific protease inhibitor-ovomucoid from whites of duck eggs--in the bulk of polymeric hydrogel. The sorbents were shown to exhibit high capacity and selectivity in the removal of proteases from the model protein-containing solutions, blood plasma and blood. The sorbents did not affect the blood cells as well as the blood-clotting system. The sorbents were demonstrated to be effective in the removal of proteases from canine blood in acute pancreatitis.

Acute Disease↗