Zobrazeno 1 - 10
of 155
pro vyhledávání: '"Ross T. A. MacGillivray"'
Publikováno v:
Nutrients, Vol 5, Iss 7, Pp 2289-2313 (2013)
Multi-copper oxidases (MCOs) are a small group of enzymes that oxidize their substrate with the concomitant reduction of dioxygen to two water molecules. Generally, multi-copper oxidases are promiscuous with regards to their reducing substrates and a
Externí odkaz:
https://doaj.org/article/788d2fe997f547beaa64ed725dff5158
Publikováno v:
Journal of Thrombosis and Haemostasis. 18:2054-2056
Autor:
Franziska L. Lederer, Robert Braun, Katrin Pollmann, Katrin Flemming, Nora Schönberger, Falk Lehmann, Sabine Matys, Susan B. Curtis, Ross T. A. MacGillivray, Stefanie Bachmann
Publikováno v:
Solid State Phenomena. 262:443-446
The development of effective and ecofriendly processes for the recovery of critical elements poses a challenge for scientists all over the world. A novel approach is the generation of highly specific peptides that bind with high affinity to individua
Autor:
Susan B. Curtis, Ross T. A. MacGillivray, Stefanie Bachmann, Franziska L. Lederer, W. Scott Dunbar
Publikováno v:
Biotechnology and Bioengineering. 114:1016-1024
As components of electronic scrap, rare earth minerals are an interesting but little used source of raw materials that are highly important for the recycling industry. Currently, there exists no cost-efficient technology to separate rare earth minera
Publikováno v:
Biotechnology and Bioengineering. 114:998-1005
Innovative approaches to the separation of minerals and subsequent extraction of metals are imperative owing to the increasing mineralogical complexity of ore deposits that are difficult or even impossible to separate into slurries or solutions conta
Publikováno v:
Nutrients, Vol 5, Iss 7, Pp 2289-2313 (2013)
Nutrients
Nutrients
Multi-copper oxidases (MCOs) are a small group of enzymes that oxidize their substrate with the concomitant reduction of dioxygen to two water molecules. Generally, multi-copper oxidases are promiscuous with regards to their reducing substrates and a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::851b11f0027c311d1223c7b0bf73d706
Publikováno v:
Dalton transactions (Cambridge, England : 2003). 47(41)
The coordination environment of Cm(iii) bound at the Fe(iii) binding sites of transferrin was investigated using a combined experimental and theoretical approach. Complexation studies with two hTf/2N single point mutants, Y95F (Tyr → Phe) and H249A
Publikováno v:
Dalton Transactions. 44:1850-1857
The complexation of Cm(III) with the recombinant N-lobe of human serum transferrin (hTf/2N) is investigated in the pH range from 4.0 to 11.0 using TRLFS. At pH ≥ 7.4 a Cm(III) hTf/2N species is formed with Cm(III) bound at the Fe(III) binding site.
Publikováno v:
Vascular Diseases and Therapeutics. 2
Autor:
Franziska L, Lederer, Susan B, Curtis, Stefanie, Bachmann, W Scott, Dunbar, Ross T A, MacGillivray
Publikováno v:
Biotechnology and bioengineering. 114(5)
As components of electronic scrap, rare earth minerals are an interesting but little used source of raw materials that are highly important for the recycling industry. Currently, there exists no cost-efficient technology to separate rare earth minera