2002
DOI: 10.1006/abio.2001.5603
|View full text |Cite
|
Sign up to set email alerts
|

Activation of Cellulose Membranes with 1,1′-Carbonyldiimidazole or 1-Cyano-4-dimethylaminopyridinium tetrafluoroborate as a Basis for the Development of Immunosensors

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

0
40
0
2

Year Published

2006
2006
2015
2015

Publication Types

Select...
7
1

Relationship

0
8

Authors

Journals

citations
Cited by 44 publications
(42 citation statements)
references
References 15 publications
0
40
0
2
Order By: Relevance
“…This strategy avoid the presence of some carbonyl groups on the surface of the monolayer that could induce non-specific protein adsorption [36].…”
Section: Discussionmentioning
confidence: 99%
“…This strategy avoid the presence of some carbonyl groups on the surface of the monolayer that could induce non-specific protein adsorption [36].…”
Section: Discussionmentioning
confidence: 99%
“…The activity of the immobilized GOD could be measured using a photometric activity assay via the produced H 2 O 2 from a peroxidase coupled coloring reaction (Stöllner et al, 2002). This measurement revealed that 0.4 mU GOD was immobilized on the electrode surface.…”
Section: Characteristics Of the Silica/godmentioning
confidence: 99%
“…The apparent enzyme activities of the entrapped GOD were determined via the produced H 2 O 2 by a coupled peroxidase color reaction (Stöllner et al, 2002). Photometric measurements were performed with a Cary 5E UV-vis-NIR spectrophotometer.…”
Section: Apparatusmentioning
confidence: 99%
“…Furthermore, the activity of the bound and released GOx was determined via the produced H 2 O 2 by a coupled peroxidase color reaction [25]. Our measurements reveal that 0.075 nU of the bound GOx is released by the incubation in the sorbitol solution and 0.188 nU of GOx still remains on the modified GC electrode, $ 28.5% of the total bound GOx is replaced by sorbitol.…”
Section: Affinity Interaction Of Gox With the Poly-apba Filmmentioning
confidence: 99%
“…The apparent enzyme activities of bound and released GOx were determined from the produced H 2 O 2 by a coupled peroxidase color reaction [25]. To determine the released GOx, first we incubated the GOx-modified electrode in 300 lL of 0.1 M sorbitol + 0.1 M pH 7.5 PBS for 20 min and then removed the electrode; then we added 700 lL of 0.1 M pH 5.0 PBS containing 0.1 mg mL À1 TMB + 50 mM D(+)glucose + 25 lg ml À1 HRP into the incubated solution and rapidly mixed the solution.…”
Section: Photometric Activity Assaymentioning
confidence: 99%