Evidence map›Paper›PMID 8856941›Full record

ReviewApplied biochemistry and biotechnology1996

Antigen-antibody binding kinetics for biosensors. Changes in the fractal dimension (surface roughness) and in the binding rate coefficient.

A Sadana, A B Ram

Abstract readReview
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In one paragraph

Review in Applied biochemistry and biotechnology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.0field-weighted citation impact, top 23% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 4 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

A SadanaChemical Engineering Department, University of Mississippi, University 38677-9740, USA.
A B Ram
University of Mississippi · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The diffusion-limited binding kinetics of antigen in solution to antibody immobilized on a biosensor surface is analyzed within a fractal framework. Changes in the fractal dimension, Df observed are in the same and in the reverse directions as the forward binding rate coefficient k. For example, an increase in the concentration of the isoenzyme human creatine kinase isoenzyme MB form (CK-MB) (antigen) solution from 0.1 to 50 ng/mL and bound to anti-CK-MB antibody immobilized on fused silica fiber rods leads to increases in the fractal dimension Df from 0.294 to 0.5080, and in the forward binding rate coefficient k from 0.1194 to 9.716, respectively. The error in the fractal dimension Df decreases with an increase in the CK-MB isoenzyme concentration in solution. An increase in the concentration of human chorionic gonadotrophin (hCG) in solution from 4000 to 6000 mIU/mL hCG and bound to anti-hCG antibody immobilized on a fluorescence capillary fill device leads to a decrease in the fractal dimension Df from 2.6806 to 2.6164, and to an increase in the forward binding rate coefficient k from 3.571 to 4.033, respectively. The different examples analyzed and presented together indicate one means by which the forward binding rate coefficient k may be controlled, that is by changing the fractal dimension or the "disorder' on the surface. The analysis should assist in helping to improve the stability, the sensitivity, and the response time of biosensors.

Indexed as

Antigen-Antibody ReactionsBiosensing TechniquesFractalsAntibodiesChorionic GonadotropinCreatine KinaseHumansIsoenzymesKineticsModels, ImmunologicalAntibodiesChorionic GonadotropinCreatine KinaseIsoenzymes

Identifiers

PMID8856941
OpenAlexW2080306355

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.