Zobrazeno 1 - 10
of 80
pro vyhledávání: '"P.O. Nyman"'
Publikováno v:
Protein Expression and Purification. 4:149-159
Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase), widespread in nature with a crucial role in the nucleotide metabolism, catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate. The enzyme from herpes simplex virus type 1 (HSV-1 dUTPase)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a6e7169f5de915e049405418aeae392
https://doi.org/10.1006/prep.1993.1021
https://doi.org/10.1006/prep.1993.1021
Autor:
T. Johansson, P.O. Nyman
Publikováno v:
Archives of Biochemistry and Biophysics. 300:49-56
The basidiomycete Trametes versicolor is a white-rot fungus and a potent degrader of lignin. The development of extracellular enzyme activities in the fungal culture under physiological conditions of secondary metabolism was investigated. Using the c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9a9c785139d0f702310ec60e53966781
https://doi.org/10.1006/abbi.1993.1007
https://doi.org/10.1006/abbi.1993.1007
Publikováno v:
Archives of Biochemistry and Biophysics. 300:57-62
The basidiomycete Trametes versicolor, a white-rot fungus and potent degrader of lignin, produces multiple forms of extracellular peroxidases. Nine of these forms, six lignin peroxidases and three manganese(II) peroxidases, purified as described in t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cffe24dffd6736414b560ad9fd935fc3
https://doi.org/10.1006/abbi.1993.1008
https://doi.org/10.1006/abbi.1993.1008
Autor:
P.O. Nyman
Publikováno v:
International Journal of Control. 54:393-415
A fundamental role in the equalizing approach ℋ∞ to optimal control is assumed by solutions which together with a related spectral density satisfy the so-called equalizer principle, a sufficient condition for minimality of the largest singular va
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::67e605c09e6bf3ebd88a10421e27443d
https://doi.org/10.1080/00207179108934166
https://doi.org/10.1080/00207179108934166
Publikováno v:
FEBS Letters. 48:167-171
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5575e2ae6271f3042ec023fec55a8aac
https://doi.org/10.1016/0014-5793(74)80459-x
https://doi.org/10.1016/0014-5793(74)80459-x
Publikováno v:
Journal of Biological Chemistry. 251:5457-5463
The primary structure of human erythrocyte carbonic anhydrase C has been determined. The single polypeptide chain contains 259 amino acid residues devoid of disulfide bridges. The experimental approach has involved restriction of the action of trypsi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f08daa8db416e49dad899cef053a2071
https://doi.org/10.1016/s0021-9258(17)33081-8
https://doi.org/10.1016/s0021-9258(17)33081-8
Publikováno v:
FEBS Letters. 24:229-235
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2fcb56dd87ddb5965c85602927068a3
https://doi.org/10.1016/0014-5793(72)80773-7
https://doi.org/10.1016/0014-5793(72)80773-7
Autor:
P.O. Nyman, P.O. Göthe, P.-C. Bergstén, K.K. Kannan, K. Fridborg, M. Petef, L. Adler, I. Waara, S. Lövgren, B. Strandberg, Anders Liljas, S.O. Falkbring
Publikováno v:
Journal of Molecular Biology. 63:601-604
Human carbonic anhydrase B has been crystallized from 2.3 m -ammonium sulphate solution at pH 8.7. A method for reproducible crystallization is presented. The crystals are suitable for high-resolution X-ray diffraction studies. They belong to the ort
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e6474a8c98df2d8d2c14a8ce08c3319b
https://doi.org/10.1016/0022-2836(72)90452-4
https://doi.org/10.1016/0022-2836(72)90452-4
Publikováno v:
Journal of Molecular Biology. 5:IN8-584
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1d8a28d7580b392283a2f9dca8250ec7
https://doi.org/10.1016/s0022-2836(62)80135-1
https://doi.org/10.1016/s0022-2836(62)80135-1