Article Abstract:
The binding ability of Aeromonas hydrophila to iron-containing glcoproteins, lactorferrin, ferritin, cyctochrome c, hemin and transferrin was investigated. Results showed that the binding was specific and reversible. However the binding ability was reduced when the bacterial population was treated with pepsin and neuraminidase. Analysis showed that the glycosidic part of the lactoferrinmolecule was involved in the binding process. With other iron-containing compound, binding occurred with bacterial surface process different with lactoferrin binding. Lactoferrin binds was also influenced by culture conditions and sidephore production.
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Article Abstract:
The cellulose-binding domain (CBD) present on a noncatalytic scaffoldin subunit of the cellulosome in Clostridium thermocellum is similar in structure, substrate affinity and binding capacity to the CBD present in C. cellulovorans. However the polyclonal antibodies produced against the CBD of C. thermocellum do not act against the CBD of C. cellulovorans possibly because the exposed epitopes in the two CBD's are different. Chemical changes in the cysteine of the CBD do not affect the CBD's ability to bind cellulose.
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Article Abstract:
Lactoferrin suppresses translocation of bacteria probably by reducing their growth in the intestines of mice fed with bovine milk. Oral administration of bovine milk to mice stimulates the translocation of bacteria such as Enterobacteriaceae from the gut to the lymph nodes. But an addition of lactoferrin or a pepsin-generated hydrolysate of lactoferrin to the milk reduces the translocation of bacteria.
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