Zobrazeno 1 - 10
of 14
pro vyhledávání: '"A A, Sereĭskaia"'
Publikováno v:
Biokhimiia (Moscow, Russia). 59(3)
Bovine fibrinogen N-terminal fragments were hydrolyzed by native alpha-thrombin and its nonclotting gamma-form with an additional disrupted anion-binding exosite (ABE). The susceptible bond 19-20 of the bovine fibrinogen A alpha-chain was found to be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fffedd654c93a5d294e4f4347cd05605
https://pubmed.ncbi.nlm.nih.gov/8180269
https://pubmed.ncbi.nlm.nih.gov/8180269
Publikováno v:
Biokhimiia (Moscow, Russia). 55(4)
The ability of native alpha- and non-coagulating gamma-thrombin to catalyze the hydrolysis of nonspecific high molecular weight substrates was studied using chymotrypsinogen and the oxidized insulin B-chain as substrates. The effect of thrombin on ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2b06d04d90afa1238e2f1cd177a385f6
https://pubmed.ncbi.nlm.nih.gov/2198949
https://pubmed.ncbi.nlm.nih.gov/2198949
Publikováno v:
Biokhimiia (Moscow, Russia). 47(4)
The kinetic parameters of hydrolysis of methyl esters of N alpha-arylsulfonyl-arginine and N-arylsulfonyl-valyl-arginine by alpha- and beta/gamma-thrombins were calculated. It was found that the polarity and volume of arylsulfonyl substitute are esse
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d45a90f3cfb7986b71ebc005fba96b8c
https://pubmed.ncbi.nlm.nih.gov/7082687
https://pubmed.ncbi.nlm.nih.gov/7082687
Publikováno v:
Biokhimiia (Moscow, Russia). 51(10)
It was shown that selective hydrolysis of the disulfide bridge between the A- and B-chains of human thrombin in the absence of denaturating agents decrease its proteolytic (e.g., fibrinogen-binding), esterase and amidase activities. Both chains remai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::66cb869d06fd02ce2f936ce7c47210e0
https://pubmed.ncbi.nlm.nih.gov/3778971
https://pubmed.ncbi.nlm.nih.gov/3778971
Publikováno v:
Biokhimiia (Moscow, Russia). 43(4)
The N(alpha)-arylsulfonyl-L-arginine ethyl- and propyl esters were synthesized and the kinetics of their hydrolysis by thrombin was studied. The values of kcat and Km were shown to depend on the structure of the leaving group and to decrease in the l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::411a39a05d47cf469497c932c3a3c785
https://pubmed.ncbi.nlm.nih.gov/656499
https://pubmed.ncbi.nlm.nih.gov/656499
Publikováno v:
Biokhimiia (Moscow, Russia). 42(9)
For comparative studies on the esterase activities of thrombin and trypsin N(alpha)-arylsulfonyl-L-arginine methyl esters were synthetised containing in aromatic ring substituents of different polar nature, size and hydrophobicity. The kinetics of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c249e9902551985fca7bb2c496f67cc1
https://pubmed.ncbi.nlm.nih.gov/20997
https://pubmed.ncbi.nlm.nih.gov/20997
Publikováno v:
Biokhimiia (Moscow, Russia). 40(1)
Trypsin- and thrombin-catalysed hydrolysis of the Nalpha-aryl-sulfonyl-L-arginine methyl esters was studied. Michaelis constants and kcat were determined. The hydrolysis of the substrates by trypsin appears to depend on the polar nature of substitute
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::155c582b8ab2645a7fb1af6841262bfd
https://pubmed.ncbi.nlm.nih.gov/166707
https://pubmed.ncbi.nlm.nih.gov/166707
Publikováno v:
Biokhimiia (Moscow, Russia). 54(4)
The A- and B-chains have been isolated from the non-covalent complex of human thrombin A- and B-chains, using selective reduction of the interchain disulfide bridge. The B-chain thus isolated (de-A-thrombin) retains its conformation, which is close t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0df1cbec361b6d7a242b4151fa8afb70
https://pubmed.ncbi.nlm.nih.gov/2758067
https://pubmed.ncbi.nlm.nih.gov/2758067
Publikováno v:
Biokhimiia (Moscow, Russia). 50(8)
It was demonstrated that partial reduction of disulfide bonds in thrombin by dithiothreitol in the absence of denaturating agents leads to a decrease of enzymatic activity with respect to fibrinogen coagulation and tosylarginine methyl ester hydrolys
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b056977493525c418e13d24855240540
https://pubmed.ncbi.nlm.nih.gov/4074791
https://pubmed.ncbi.nlm.nih.gov/4074791
Publikováno v:
Ukrainskii biokhimicheskii zhurnal (1. 55(3)
Partial dithiothreitol-reduction of the disulphide thrombin bonds when denaturating agents are absent lowers significantly enzymic activity of thrombin relative to fibrinogen coagulation. This permits supposing that at least one of the disulphide bri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::04db330243d1adf498bebf49952d3155
https://pubmed.ncbi.nlm.nih.gov/6868151
https://pubmed.ncbi.nlm.nih.gov/6868151