Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Andrew G. Popplewell"'
Autor:
Andrew G. Popplewell
Publikováno v:
Pharmaceutical Sciences Encyclopedia
The development of recombinant DNA methodology and genetic engineering from the late 1970s onwards opened up a range of possibilities for making specific changes to primary protein sequences. This chapter serves as an introduction to protein engineer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8371cc074452c9da87d1836d8362cc0e
https://doi.org/10.1002/9780470571224.pse537
https://doi.org/10.1002/9780470571224.pse537
Publikováno v:
Transgenic Research. 5:87-95
Transgenic tilapia were produced using a carp β-actinlacZ gene construct and the transmission of the transgene to F1 progeny was followed. Of 36 founder fish analysed, 9 (25%) were found to be transgenic in at least one tissue and two of these were
Autor:
James T, Heads, Ralph, Adams, Lena E, D'Hooghe, Matt J T, Page, David P, Humphreys, Andrew G, Popplewell, Alastair D, Lawson, Alistair J, Henry
Publikováno v:
Protein science : a publication of the Protein Society. 21(9)
The stability of therapeutic antibodies is a prime pharmaceutical concern. In this work we examined thermal stability differences between human IgG1 and IgG4 Fab domains containing the same variable regions using the thermofluor assay. It was found t
Autor:
Tommy Wan, Michael D. Scawen, Andrew G. Popplewell, Stephen P. Bottomley, Brian J. Sutton, Michael G. Gore
Publikováno v:
"Protein Engineering, Design and Selection". 7:1463-1470
The stability and unfolding of an immunoglobulin (Ig) G binding protein based upon the B domain of protein A (SpAB) from Staphylococcus aureus were studied by substituting tryptophan residues at strategic locations within each of the three alpha-heli
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1202:235-243
The glycerol dehydrogenase (GDH) from Bacillus stearothermophilus is inactivated by incubation with pyridoxal-5-phosphate (PALP). The complex formed between the two can be trapped by reduction with sodium borohydride to yield a protein with an absorb
A single-immunoglobulin-binding protein based upon the C2 domain of Protein G from Streptococcus has been shown to bind tightly to the Fc fragment of IgG1. The binding interaction results in a decrease in the fluorescence intensity from the sole Trp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2534ca8daa6c3673d913bd6ea501833
https://europepmc.org/articles/PMC1135870/
https://europepmc.org/articles/PMC1135870/
Publikováno v:
Protein engineering. 5(6)
A fusion protein, consisting of the N-terminal 81 amino acids from an inactive bovine DNase I (Q38,E39-E38,Q39) and two sequential synthetic IgG-binding domains based upon domain B of Protein A from Staphylococcus aureus has been shown to bind to por
Publikováno v:
Protein engineering. 4(8)
A novel protein able to bind with high affinity to the Fc fragment of IgG from a variety of animals has been produced by a gene synthesis approach. The IgG binding is accomplished by the presence of a single or two consecutive domains based upon doma
Autor:
Tony Atkinson, Andrew G. Popplewell, Michael G. Gore, Lisa J. Paine, Ruth Burton, Paul Charlton
Publikováno v:
Biochemical Society Transactions. 20:259S-259S
Publikováno v:
Biochemical Society Transactions. 20:288S-288S