Zobrazeno 1 - 10
of 18
pro vyhledávání: '"T I, Nikolaeva"'
Publikováno v:
Science and Education a New Dimension. :10-13
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8a42c0cecdf2da01251cf8cd8430f53a
https://doi.org/10.31174/send-hs2019-214vii36-02
https://doi.org/10.31174/send-hs2019-214vii36-02
Publikováno v:
Bulletin of Experimental Biology and Medicine. 165:629-634
Enzymatic hydrolysis of biopolymers of the cartilage tissue was studied for obtaining a complex of type II collagen peptides and glycosaminoglycan oligosaccharides. Hydrothermal hydrolysis in a high pressure homogenizer followed by enzymatic hydrolys
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad265deb39b2a56c1d9040531460099c
https://doi.org/10.1007/s10517-018-4229-0
https://doi.org/10.1007/s10517-018-4229-0
Publikováno v:
Bulletin of experimental biology and medicine. 167(2)
We studied the effects of Chymopsin and Caripazim on the proteolysis of collagen proteins from cattle tracheal hyaline cartilage. Homogenization of the cartilage under conditions of high pressure and temperature facilitated subsequent enzymatic hydro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::385ab267d52bf0bb7090e502ea6dacee
https://pubmed.ncbi.nlm.nih.gov/31243681
https://pubmed.ncbi.nlm.nih.gov/31243681
Publikováno v:
Biophysics. 57:757-763
Fibril formation by collagen from piglet skin was studied at temperatures of 28–39°C. Collagen fibrils obtained in this temperature range differ in the degree of ordering. Electron microscopy shows that fibrils of minimal diameter are formed at ph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d29022fb765dd7b24062d2059eeec6a8
https://doi.org/10.1134/s0006350912060139
https://doi.org/10.1134/s0006350912060139
Publikováno v:
Biophysics. 52:489-497
Reviewed are works concerning the mechanisms of collagen (type I) fibril packing and the influence of macromolecular structure and physicochemical parameters of the medium on the process.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f231373e27a94e0bfc9e3ace264d8ede
https://doi.org/10.1134/s0006350907050065
https://doi.org/10.1134/s0006350907050065
Publikováno v:
Biophysics. 52:191-195
Analysis of the results of calorimetric study of reconstituted collagen (type I) fibrils, in particular, the half-width of the temperature transition, shows that the collagen packing density in the fibrils and the size of cooperative blocks therein d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1f2e509203f4fc3b75f9acb69b691232
https://doi.org/10.1134/s000635090702008x
https://doi.org/10.1134/s000635090702008x
Publikováno v:
Biophysics. 54:683-685
The data on the effect of temperature on the kinetics of collagen fibril formation at physiological pH values and ionic strength in the temperature range 26–39°C have been analyzed. The temperature of 35°C optimal for collagen fibril formation ha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::282bfdcc15210b5fe0c63d6a41b8e5f4
https://doi.org/10.1134/s0006350909060049
https://doi.org/10.1134/s0006350909060049
Publikováno v:
Biofizika. 57(6)
Fibril formation of collagen from porcine skin was studied at temperatures of 28-39 degrees C. Collagen fibrils obtained in this temperature range have the different degree of order. An optimal temperature for the formation of collagen fibrils is fou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8023bf12de40bee8cf7d794471927c18
https://pubmed.ncbi.nlm.nih.gov/23272577
https://pubmed.ncbi.nlm.nih.gov/23272577
Publikováno v:
Biofizika. 54(6)
The data on the effect of temperature on the kinetics of collagen fibril formation at physiological pH values and ionic strength in the temperature range 26-39 degrees C have been analyzed. The temperature of 35 degrees C optimal for collagen fibril
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c0ef915639f48331872629e9ad8009bb
https://pubmed.ncbi.nlm.nih.gov/20067180
https://pubmed.ncbi.nlm.nih.gov/20067180
Publikováno v:
Biofizika. 52(5)
Studies devoted to the analysis of the mechanisms of packing of collagen fibrils and the effect of the macromolecular structure and the physicochemical parameters of medium on the packing are reviewed.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6d070d3c7ea211f909b67357ab3c8123
https://pubmed.ncbi.nlm.nih.gov/17969926
https://pubmed.ncbi.nlm.nih.gov/17969926