Zobrazeno 1 - 10
of 11
pro vyhledávání: '"G B, Villanueva"'
Publikováno v:
Archives of Biochemistry and Biophysics. 300:302-308
Escherichia coli DNA topoisomerase I contains three Zn(II) in each enzyme molecule required for relaxation of negatively supercoiled DNA. Apoenzymes were prepared from both the intact topoisomerase (M(r) 97,000) and the truncated active form top85 (M
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::84338399b68b24ae411fc968f9a2fa26
https://doi.org/10.1006/abbi.1993.1042
https://doi.org/10.1006/abbi.1993.1042
Publikováno v:
Biochemistry and molecular biology international. 33(5)
The surface binding activity of human coagulation factor XII is independent of pH while its proteolytic breakdown decreases considerably on lowering the pH (Samuel, M. and Villanueva, G.B. (1992) Biophysical J. 61, 1895). In the present study we show
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7daa6b0fc45f3bc19124adf4a864948a
https://pubmed.ncbi.nlm.nih.gov/7987251
https://pubmed.ncbi.nlm.nih.gov/7987251
Publikováno v:
The Journal of biological chemistry. 267(27)
The first event leading to the activation of the plasma kallikrein-kinin system is the surface-dependent conversion of factor XII to an active enzyme. Factor XII autoactivation was investigated using dextran sulfate as a soluble activating surface, a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9662899b38e4516215d5bd9facac35d7
https://pubmed.ncbi.nlm.nih.gov/1527088
https://pubmed.ncbi.nlm.nih.gov/1527088
Autor:
N Allen, G B Villanueva
Publikováno v:
Journal of Biological Chemistry. 258:11010-11013
The denaturation of human antithrombin III in urea and guanidinium chloride (GdmCl) was investigated by intrinsic fluorescence, circular dichroism, and absorption difference spectroscopy. Results suggest the existence of two structural domains as evi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4a75c5ec30568910fc2ddce3bcedcc7b
https://doi.org/10.1016/s0021-9258(17)44378-x
https://doi.org/10.1016/s0021-9258(17)44378-x
Autor:
G B Villanueva, N Allen
Publikováno v:
Journal of Biological Chemistry. 258:14048-14053
The presence of two unfolding domains in antithrombin III during its denaturation in guanidinium chloride has previously been reported (Villanueva, G. B., and Allen, N. (1983) J. Biol. Chem. 258, 11010-11013). In the present work, we report the resul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::751b041b981f2ee5ae799d7206a5b5ab
https://doi.org/10.1016/s0021-9258(17)44022-1
https://doi.org/10.1016/s0021-9258(17)44022-1
Autor:
G. B. Villanueva, N. Allen
Publikováno v:
Diabetes. 37:1103-1107
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4e54c6ea9aad25e07aba12d354d57644
https://doi.org/10.2337/diabetes.37.8.1103
https://doi.org/10.2337/diabetes.37.8.1103
Autor:
G B Villanueva
Publikováno v:
Journal of Biological Chemistry. 259:2531-2536
The secondary structure of antithrombin III was investigated using the predictive scheme based on the amino acid sequence (Fasman, G. D., Chou, P. Y., and Adler, A. J. (1976) Biophys. J. 16, 1201-1238. The relative composition of the conformational r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4e27f82dc3447711504cad1abacf8ac2
https://doi.org/10.1016/s0021-9258(17)43385-0
https://doi.org/10.1016/s0021-9258(17)43385-0
Publikováno v:
Chemischer Informationsdienst. 6
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3371d703335e190887a66dcd9bfb2e03
https://doi.org/10.1002/chin.197501437
https://doi.org/10.1002/chin.197501437
Autor:
G B, Villanueva
Publikováno v:
The Journal of biological chemistry. 259(4)
The secondary structure of antithrombin III was investigated using the predictive scheme based on the amino acid sequence (Fasman, G. D., Chou, P. Y., and Adler, A. J. (1976) Biophys. J. 16, 1201-1238. The relative composition of the conformational r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::80a80c8eb099e44793a70903b130ff05
https://pubmed.ncbi.nlm.nih.gov/6698980
https://pubmed.ncbi.nlm.nih.gov/6698980
Autor:
G B, Villanueva, N, Allen
Publikováno v:
The Journal of biological chemistry. 258(22)
The presence of two unfolding domains in antithrombin III during its denaturation in guanidinium chloride has previously been reported (Villanueva, G. B., and Allen, N. (1983) J. Biol. Chem. 258, 11010-11013). In the present work, we report the resul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a1c6a18752d427f056dfefa0d3b408f6
https://pubmed.ncbi.nlm.nih.gov/6643466
https://pubmed.ncbi.nlm.nih.gov/6643466