|
pubmed:abstractText |
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.
|
