Relative stabilities of IgG1 and IgG4 Fab domains: influence of the light-heavy interchain disulfide bond architecture
about
Understanding the relationship between biotherapeutic protein stability and solid-liquid interfacial shear in constant region mutants of IgG1 and IgG4A comparison of biophysical characterization techniques in predicting monoclonal antibody stability.A mixture of functionally oligoclonal humanized monoclonal antibodies that neutralize Clostridium difficile TcdA and TcdB with high levels of in vitro potency shows in vivo protection in a hamster infection model.Aggregation and chemical modification of monoclonal antibodies under upstream processing conditions.Temperature denaturation and aggregation of a multi-domain protein (IgG1) investigated with an array of complementary biophysical methods.
P2860
Relative stabilities of IgG1 and IgG4 Fab domains: influence of the light-heavy interchain disulfide bond architecture
description
2012 nî lūn-bûn
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2012年の論文
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2012年学术文章
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2012年学术文章
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2012年学术文章
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2012年学术文章
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2012年學術文章
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name
Relative stabilities of IgG1 a ...... in disulfide bond architecture
@en
Relative stabilities of IgG1 a ...... n disulfide bond architecture.
@nl
type
label
Relative stabilities of IgG1 a ...... in disulfide bond architecture
@en
Relative stabilities of IgG1 a ...... n disulfide bond architecture.
@nl
prefLabel
Relative stabilities of IgG1 a ...... in disulfide bond architecture
@en
Relative stabilities of IgG1 a ...... n disulfide bond architecture.
@nl
P2093
P2860
P356
P1433
P1476
Relative stabilities of IgG1 a ...... in disulfide bond architecture
@en
P2093
Alastair D Lawson
Alistair J Henry
Andrew G Popplewell
David P Humphreys
James T Heads
Lena E D'Hooghe
Matt J T Page
Ralph Adams
P2860
P304
P356
10.1002/PRO.2118
P577
2012-08-09T00:00:00Z