Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Ciarán Ó Fágáin"'
Autor:
Ann Murphy, Ciarán Ó Fágáin
Publikováno v:
Biotechnology and Bioengineering. 58:366-373
Bovine pancreatic trypsin was treated with ethylene glycol bis(succinic acid N-hydroxysuccinimide ester). Approximately 8 of 14 lysines per trypsin molecule were modified. This derivative (EG trypsin) was more stable than native between 30 degrees an
Autor:
JoséM. Moreno, Ciarán Ó Fágáin
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 2:271-279
Alanine aminotransferase (ALT) is used in clinical diagnostics, amino acid synthesis and in biosensors. Here we describe the stabilization of soluble porcine ALT by chemical modification with mono- and bis-imidates. The apparent transition temperatur
Publikováno v:
Analytical Chemistry. 69:1674-1681
Amperometric organic- and aqueous-phase peroxide biosensors were prepared with native and N-hydroxysuccinimide ester (NHS)-modified horseradish peroxidase (HRP). The e-amino functions of the free lysine residues of HRP were selectively modified with
Autor:
Ann Murphy, Ciarán Ó Fágáin
Publikováno v:
Biotechnology Techniques. 11:13-16
A modified trypsin (AA-trypsin, acetylated with acetic acid N-hydroxysuccinimide ester) gave increased yields of Bzl-Arg-Leu-NH2 dipeptide (90% versus 59% for native trypsin) when used in 95% acetonitrile. AA-Trypsin had decreased Km and increased kc
Publikováno v:
Journal of Chemical Technology & Biotechnology. 67:227-236
Horseradish peroxidase (HRP) catalyses the oxidation of toxic aromatic compounds, especially phenols, in the presence of hydrogen peroxide. Reaction products polymerise to form insoluble precipitates which readily separate from aqueous solution, unli
Autor:
Ciarán Ó Fágáin, José M. Moreno
Publikováno v:
Biotechnology Letters. 18:51-56
A new combination of methodologies for enzyme stabilization has been carried out. Dimethylsuberimidate-modified alanine aminotransferase was covalently immobilized on a preactivated agarose gel. The resulting derivative showed greater residual activi
Publikováno v:
Thrombosis Research. 80:247-254
Factor VIII performs a critical role in the blood coagulation cascade but is extremely labile. We have carried out chemical studies on a fully functional recombinant Factor VIII (rFVIII) using a variety of protein modifying agents, some of which were
Autor:
Ciarán Ó Fágáin
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1252:1-14
This review surveys the processes leading to loss of protein function and the types of molecular interaction that help stabilize proteins. It considers the effects of organic solvents on stability and the special features of thermophilic proteins. Th
Autor:
Deborah M. Ruth, Ciarán Ó Fágáin, Brian W. Moran, Peter T.M. Kenny, Frankie P. Anderson, John P. Dalton
Publikováno v:
Journal of enzyme inhibition and medicinal chemistry. 25(1)
Cathepsins are known to have many important physiological roles and provide a viable target for inhibition. Fluorobenzoyl dipeptide derivatives were synthesized and tested for biological activity in an effort to find an efficient inhibitor of the cys
Autor:
Ciarán Ó Fágáin, Richard O'Kennedy
Publikováno v:
Biotechnology Advances. 9:351-409
The maintenance or stabilization of protein or enzyme function is of vital importance in Biotechnology. Investigations of thermophilic organisms, studies of denaturation and the use of enzymes in organic solvents have each contributed to an understan