Zobrazeno 1 - 10
of 18
pro vyhledávání: '"R. B. Ponomareva"'
Autor:
E A, Zelepuga, R B, Ponomareva, V M, Kolikov, V D, Pautov, T V, Sheveleva, M L, Medvedev, T M, Tret'iak, O N, Trepelovskaia
Publikováno v:
Biomeditsinskaia khimiia. 49(6)
Conjugates of pancreatic RNase and ligand-free human serum albumin (LFHSA) have been obtained. The number of hydrophobic binding sites both for initial HSA and LFHSA has been determined by the polarised luminescence method. Interaction between RNase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::75ab4d7c140518bf11fecdcb62823510
https://pubmed.ncbi.nlm.nih.gov/16119087
https://pubmed.ncbi.nlm.nih.gov/16119087
Publikováno v:
Prikladnaia biokhimiia i mikrobiologiia. 30(1)
The efficiency of the binding of RNase 7P molecules to albumin on cocondensation with the aim of producing the prolonged action forms of the enzyme can be increased by using ligand-free human serum albumin (LFHSA). The CD method showed that LFHSA und
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::236d0debf64c628b4c11fb2b03107437
https://pubmed.ncbi.nlm.nih.gov/8146114
https://pubmed.ncbi.nlm.nih.gov/8146114
Publikováno v:
Voprosy meditsinskoi khimii. 39(5)
Penetration of exogenous RNAases, native and albumin polymer-bound, from circulation into the brain parenchyma was studied. Native pancreatic RNAase was found to extend through the hematoencephalic barrier; maximal enzymatic activity was detected wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c5bebbf7fa33f58875fcd23223a5d24e
https://pubmed.ncbi.nlm.nih.gov/8279142
https://pubmed.ncbi.nlm.nih.gov/8279142
Publikováno v:
Voprosy meditsinskoi khimii. 36(5)
Conjugates containing blood serum albumin and pancreatic ribonuclease, produced by means of polycondensation reaction, exhibited higher half-life in rabbit circulation as compared with non-modified enzyme. Presence of the protein-carrier contributed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2e21790b18fc68c9951afbbf8c3bea7e
https://pubmed.ncbi.nlm.nih.gov/2251790
https://pubmed.ncbi.nlm.nih.gov/2251790
Publikováno v:
Pure and Applied Chemistry. 51:1409-1420
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1b623d38cd8af46f2780a6133c296669
https://doi.org/10.1351/pac197951071409
https://doi.org/10.1351/pac197951071409
Publikováno v:
Bulletin of the Academy of Sciences, USSR Division of Chemical Science. 15:425-428
1. The change in the intrinsic viscosity, mobility on a column with Sephadex, and diffusion coefficient were studied for a number of enzymes after a breakdown of their tertiary structure. A correlation was noted in the change in these characteristics
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::57b407afbf2f359c2dfc54476324a66d
https://doi.org/10.1007/bf00846098
https://doi.org/10.1007/bf00846098
Publikováno v:
Prikladnaia biokhimiia i mikrobiologiia. 17(3)
By chromatography on ultragel ACA-54 alpha-amylase was isolated from the enzymic preparation amylosubtilin G10x. As compared to the initial preparation, the specific activity of the purified enzyme per mg increased 25-fold. The major physico-chemical
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::951264b9a1aa522286bc27e9d289cbca
https://pubmed.ncbi.nlm.nih.gov/6174969
https://pubmed.ncbi.nlm.nih.gov/6174969
Publikováno v:
Prikladnaia biokhimiia i mikrobiologiia. 19(4)
The process of reactivation of acid-inactivated alpha-amylase of Bacillus subtilis in weakly alkaline media was examined. The reactivation of alpha-amylase immobilized on carboxyl polyelectrolytes developed in a larger measure than that of the native
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a48b4ea3a2a6ac704e98df9ea2d59d16
https://pubmed.ncbi.nlm.nih.gov/6413970
https://pubmed.ncbi.nlm.nih.gov/6413970
Publikováno v:
Biokhimiia (Moscow, Russia). 40(3)
Carboxymethylcellulose, carboxymethylchitin, sulfoethylcellulose and dextrane sulfate interact with pancreatic ribonuclease. In comparison with ribonuclease activity the activity of formed complexes changes differently at the stages of transesterific
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e58cc5ca94270acaceed13bc82dfedf7
https://pubmed.ncbi.nlm.nih.gov/1107
https://pubmed.ncbi.nlm.nih.gov/1107
Publikováno v:
Biofizika. 33(6)
Effect of complex formation with dextran sulfate (DS) (substitution degree 1.3, molecular mass 500 thousand) on RNAse enzymic activity. its spatial structure and conformation stability was studied. Hydrolytic activity of the enzyme in complex in inhi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1ac2b405167477c715f4c9a4cada5c26
https://pubmed.ncbi.nlm.nih.gov/2470413
https://pubmed.ncbi.nlm.nih.gov/2470413