[A model for assessing and correcting the risk of developing pressure ulcers in the system of long-term care for geriatric patients with limited mobility.].

The article is devoted to the results of the third stage of the scientific and practical project on the introduction of advanced social practices based on innovative gerontotechnologies into the system of long-term care for geriatric patients. It has been established that senile xerosis or skin «frailty» occurs in 75% of the population over 65 years old, when increased dryness of the skin leads to peeling, the formation of microcracks, the appearance of senile itching, sleep disturbances, the development of pressure ulcers and, as a result, a decrease in motor activity. During the project, a tactic was developed for the care of «frail» skin in patients with senile xerosis and the risk of pressure ulcers.

[Current problems of polypharmacy in geriatric patients when taking drugs with a risk of photosensitivity.].

The article presents an overview of the current problems of polypharmacy in geriatric patients when taking drugs with a risk of photosensitivity. The article contains information about emerging adverse drug reactions, as well as methods for diagnosing, correcting and preventing phototoxic and photoallergic reactions in patients of older age groups. The main aspects of dermatological support in the system of long-term care for geriatric patients when taking drugs with a risk of photosensitivity are outlined.

[Social interactions in long-term care.].

Modern society is becoming more and more complex, not only technologies are changing, but also its socio-age structure. For the first time, mankind found itself in a situation where there are more elderly people than young people, and it turned out to be not ready for this. A new task arises - the coordination of interactions and interests of many subjects of social interaction in the interests of the elderly.

[Creation of a polyenzyme composition of proteases from Streptomyces griseus and Acremonium chrysogenum].

Proteolytic enzymes of microorganisms have been studied for the possibility to create their polyenzymic composition in order to rise a degree of protein hydrolysis and to lower the process duration. Optimal action conditions are selected and a hydrolysis of a number of globular and fibrillar proteins is conducted by a polyenzymic system of Streptomyces griseus and Acremonium chrysogenum proteases.

[Covalent immobilization of the pancreatic trypsin inhibitor on a polymeric carrier].

Covalent immobilization of the pancreatic trypsin inhibitor onto a polymeric carrier was accomplished by introducing a double C = C bond in the inhibitor with a subsequent copolymerization of the activized inhibitor with acrylamide and N,N'-methylenebisacrylamide. To prevent a loss of the antitryptic activity under acylation of lysine residues of the reactive centre, the inhibitor was preliminary bound to a complex with trypsin, which was destructed by acidifying the solution before copolymerization. The antitryptic activity of the immobilized inhibitor was shown to be equal to the activity of the inhibitor in the native state.

[Isolation of protein of the chymotrypsin inhibitor from honey locust seeds].

The chymotrypsin inhibitor was isolated from honey locust (Gleditsia triacanthos L.) by chromatography on trypsin- and chymotrypsin-Sepharose 4B and by gel filtration on Sephadex G-75. The inhibitor can inhibit chymotrypsin but has no effect on trypsin, subtilisin and proteinases from Asp.

[Trypsin inhibitor from Gleditsia triacanthos L. seeds].

The trypsin inhibitor from Gleditsia triacanthos (L.) seeds was purified by affinity chromatography on a column with trypsin-Sepharose 4B. The isolated inhibitor is a single-chain protein with molecular weight of about 20 000.

[Identification of the reactive sites of kidney bean proteinase inhibitor].

The protein proteinase inhibitor from kidney bean (isoinhibitor, pI 4.3) is a double-headed inhibitor with independent reactive sites for trypsin and chymotrypsin. The reactive site of the inhibitor for trypsin is Lys (22)- Ser (23) in the sequense .