Bovine lactoferrin region responsible for binding to bifidobacterial cell surface proteins.
Bovine lactoferrin promotes bifidobacterial growth. Its binding to bifidobacteria is thought to be responsible for such action. After separating the bovine lactoferrin half molecule and extraction of surface proteins from bifidobacteria, binding profiles were observed by immunoblotting. No binding appeared when lactoferrin C-lobe was reacted with the cell surface proteins on a polyvinylidene difluoride membrane. Conversely, a 50-kDa band appeared when the surface proteins were reacted with either intact or nicked bovine lactoferrin. This result strongly suggests that the binding region could be lactoferrin N-lobe. Interestingly, despite the absence of binding, C-lobe enhanced bifidobacterial growth.
Rahman
Morshedur
M
Laboratory of Dairy Food Science, Research Faculty of Agriculture, Hokkaido University, W-9, N-9, Sapporo 060-8589, Japan. morshedur68@yahoo.com
Kim
Woan-Sub
WS
Kumura
Haruto
H
Shimazaki
Kei-ichi
K
D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism*; D001644:Bifidobacterium / Q000254:growth & development / Q000378:metabolism / Q000502:physiology*; D002417:Cattle; D007781:Lactoferrin / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D011485:Protein Binding; D025941:Protein Interaction Mapping
D001426:Bacterial Proteins; D008565:Membrane Proteins; D007781:Lactoferrin