Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UNIPROT:P02794 (
ferritin
)
17,525
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Originally developed as a method for estimating the solid-phase concentration of an adsorbed protein, sequential enzyme-linked immunosorbent assay (ELISA) analysis (P. A. Underwood and J. G. Steele (1991) J. Immunol. Methods 142, 83-94) is also useful for assessing other aspects of protein-surface interactions without radioactively labeled reagents. The method provides a way to compare protein adsorption on various microwell surfaces and to track adhesion of the protein throughout an assay's wash and incubation steps. In cases where adsorption complies with Langmuir-type binding and protein desorption is minimal, sequential ELISA data can be analyzed with a mathematical model to quantitatively estimate the microwell's protein-binding capacity. Even for protein-surface interactions where the mathematical model is not appropriate, characteristics of sequential ELISA binding data qualitatively differentiate between initial adsorption with subsequent desorption and poor initial adsorption of the protein. Using this method, we analyzed the binding of three proteins (rabbit immunoglobulin G, bovine serum albumin, and horse spleen
ferritin
) to four types of polystyrene microwell surfaces (Immulons 1, 2, 3, and 4). In addition, we examined differences in protein adhesion to the four surfaces when
Tween 20
was omitted from the assay's wash buffer or when fewer washes were used.
...
PMID:Assessment of adsorption and adhesion of proteins to polystyrene microwells by sequential enzyme-linked immunosorbent assay analysis. 776 81
The gastric pathogen Helicobacter pylori has been shown to produce a 19.6-kDa protein with apparent binding activity for erythrocytes, human buccal epithelial cells, and laminin. In this report we demonstrate that it is an iron-binding protein, resembling
ferritin
both structurally and biochemically. Also, because its binding activity for laminin, erythrocytes, and buccal cells was abolished by low concentrations of
Tween 20
, binding is likely nonspecific.
...
PMID:The Helicobacter pylori 19.6-kilodalton protein is an iron-containing protein resembling ferritin. 841 4