Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Cheau Yuaan Tan"'
Publikováno v:
Journal of the Indian Chemical Society. 98:100031
In order to investigate the involvement of lysine residues of human serum albumin (HSA) in nalidixic acid (NA) binding, various modified preparations of HSA such as 44% carbamylated (C44), 83% carbamylated (C83) and 85% acetylated (A85) were made by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f67571fdf1276342d1f93fdfec0f3fd5
https://doi.org/10.1016/j.jics.2021.100031
https://doi.org/10.1016/j.jics.2021.100031
Autor:
Hidehiko Hirakawa, Risa Suzuki, Tomoaki Haga, Fumiya Iwata, Cheau Yuaan Tan, Teruyuki Nagamune
Publikováno v:
Angewandte Chemie International Edition. 55:15002-15006
Bacterial cytochrome P450s (P450s), which catalyze regio- and stereoselective oxidations of hydrocarbons with high turnover rates, are attractive biocatalysts for fine chemical production. Enzyme immobilization is needed for cost-effective industrial
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e2bc386c0f032f2ef1c09271b8dd8d2
https://doi.org/10.1002/anie.201608033
https://doi.org/10.1002/anie.201608033
Publikováno v:
Scientific Reports
Diverse applications of the versatile bacterial cytochrome P450 enzymes (P450s) are hampered by their requirement for the auxiliary proteins, ferredoxin reductases and ferredoxins, that transfer electrons to P450s. Notably, this limits the use of P45
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f87c6430964ee3db1a540708518342e9
https://pubmed.ncbi.nlm.nih.gov/25733255
https://pubmed.ncbi.nlm.nih.gov/25733255
Publikováno v:
Acta biochimica Polonica. 58(3)
Bacillus licheniformis α-amylase (BLA) was chemically modified using 100-fold molar excess of succinic anhydride over protein or 0.66 M potassium cyanate to obtain 42 % succinylated and 81 % carbamylated BLAs. Size and charge homogeneity of modified
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93de17be0d7f091f801ee06dfa720ee4
https://pubmed.ncbi.nlm.nih.gov/21887412
https://pubmed.ncbi.nlm.nih.gov/21887412