2008
|
Sign up to set email alerts
Microfluidic immunoaffinity separations for bioanalysis
Search citation statements
Order By: Relevance
Paper Sections
Select...
40
9
2
0
Citation Types
1
37
0
0
Year Published
Range
2008
20082026
2026Publication Types
Select...
43
5
3
Relationship
0
51
Authors
Journals
Cited by 51 publications
(38 citation statements)
References 86 publications
1
37
0
0
Order By: Relevance
Smart CitationsHow this paper cites the one you are viewing
“…Developed profile was similar to a typical immuno-affinity chromatogram [33]. It shows that 75.1 ± 2.2% of the total fluorescence emission (ex: 340 nm; em: 450 nm) was eluted as unabsorbed fraction while the rest was co-eluted with the peptides (Fig.…”
Section: Immuno-affinity Chromatography
supporting
confidence: 64%
Smart CitationsHow this paper cites the one you are viewing
“…Developed profile was similar to a typical immuno-affinity chromatogram [33]. It shows that 75.1 ± 2.2% of the total fluorescence emission (ex: 340 nm; em: 450 nm) was eluted as unabsorbed fraction while the rest was co-eluted with the peptides (Fig.…”
Section: Immuno-affinity Chromatography
supporting
confidence: 64%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…This difference versus the result for the Schiff base method may also reflect the more ordered orientation of antibodies in the hydrazide method, which could have made more F ab regions accessible to papain for cleavage. It should be noted that larger differences between these two immobilization methods may be observed for some types of antibodies and, in particular, monoclonal antibodies that have a relatively low degree glycosylation compared to typical polyclonal antibodies 38,39. However, this issue was not found to be a problem for the monoclonal anti-fluorescein antibodies that were used later in this current study.…”
Section: Results
mentioning
confidence: 77%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…The antigen-antibody complexes form as a result of several intermolecular forces; the five main forces are: (a) hydrogen-bonding; (b) coulombic, i.e. , electrostatic and dipole-dipole forces; (c) van der Waals; (d) hydrophobic interactions; and (e) π– π complementary ring-bonding [ 23 ]. Since adhesion forces between a small molecule and a protein are mainly non-covalent, the forces governing antigen-antibody binding are similar to that of drug-receptor binding.…”
Section: Results
mentioning
confidence: 99%
Smart CitationsHow this paper cites the one you are viewing
“…Developed profile was similar to a typical immuno-affinity chromatogram [33]. It shows that 75.1 ± 2.2% of the total fluorescence emission (ex: 340 nm; em: 450 nm) was eluted as unabsorbed fraction while the rest was co-eluted with the peptides (Fig.…”
Section: Immuno-affinity Chromatography
supporting
confidence: 64%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…This difference versus the result for the Schiff base method may also reflect the more ordered orientation of antibodies in the hydrazide method, which could have made more F ab regions accessible to papain for cleavage. It should be noted that larger differences between these two immobilization methods may be observed for some types of antibodies and, in particular, monoclonal antibodies that have a relatively low degree glycosylation compared to typical polyclonal antibodies 38,39. However, this issue was not found to be a problem for the monoclonal anti-fluorescein antibodies that were used later in this current study.…”
Section: Results
mentioning
confidence: 77%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…The antigen-antibody complexes form as a result of several intermolecular forces; the five main forces are: (a) hydrogen-bonding; (b) coulombic, i.e. , electrostatic and dipole-dipole forces; (c) van der Waals; (d) hydrophobic interactions; and (e) π– π complementary ring-bonding [ 23 ]. Since adhesion forces between a small molecule and a protein are mainly non-covalent, the forces governing antigen-antibody binding are similar to that of drug-receptor binding.…”
Section: Results
mentioning
confidence: 99%
Smart CitationsHow this paper cites the one you are viewing
“…Developed profile was similar to a typical immuno-affinity chromatogram [33]. It shows that 75.1 ± 2.2% of the total fluorescence emission (ex: 340 nm; em: 450 nm) was eluted as unabsorbed fraction while the rest was co-eluted with the peptides (Fig.…”
Section: Immuno-affinity Chromatography
supporting
confidence: 64%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…This difference versus the result for the Schiff base method may also reflect the more ordered orientation of antibodies in the hydrazide method, which could have made more F ab regions accessible to papain for cleavage. It should be noted that larger differences between these two immobilization methods may be observed for some types of antibodies and, in particular, monoclonal antibodies that have a relatively low degree glycosylation compared to typical polyclonal antibodies 38,39. However, this issue was not found to be a problem for the monoclonal anti-fluorescein antibodies that were used later in this current study.…”
Section: Results
mentioning
confidence: 77%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…The antigen-antibody complexes form as a result of several intermolecular forces; the five main forces are: (a) hydrogen-bonding; (b) coulombic, i.e. , electrostatic and dipole-dipole forces; (c) van der Waals; (d) hydrophobic interactions; and (e) π– π complementary ring-bonding [ 23 ]. Since adhesion forces between a small molecule and a protein are mainly non-covalent, the forces governing antigen-antibody binding are similar to that of drug-receptor binding.…”
Section: Results
mentioning
confidence: 99%