LACTOFERRIN/ALBUMIN FUSION PROTEIN AND PRODUCTION METHOD THEREFOR

The present invention provides a lactoferrin fusion protein having high clinical utility and a production method therefor. The present invention further provides: a lactoferrin fusion protein that retains the biological activity of native lactoferrin while having a significantly extended in vivo lif...

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Bibliographische Detailangaben
Hauptverfasser:	KAGAYA, Shinji, SATO, Atsushi
Format:	Patent
Sprache:	eng ; fre ; ger
Schlagworte:	AGRICULTURE ANIMAL HUSBANDRY BEER BIOCHEMISTRY CARE OF BIRDS, FISHES, INSECTS CHEMISTRY COMPOSITIONS THEREOF CULTURE MEDIA ENZYMOLOGY FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIREDCHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERSFROM A RACEMIC MIXTURE FISHING FORESTRY HUMAN NECESSITIES HUNTING HYGIENE MEDICAL OR VETERINARY SCIENCE METALLURGY MICROBIOLOGY MICROORGANISMS OR ENZYMES MUTATION OR GENETIC ENGINEERING NEW BREEDS OF ANIMALS ORGANIC CHEMISTRY PEPTIDES PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES PROPAGATING, PRESERVING OR MAINTAINING MICROORGANISMS REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS ORMEDICINAL PREPARATIONS SPIRITS TRAPPING VINEGAR WINE
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Beschreibung
Zusammenfassung:	The present invention provides a lactoferrin fusion protein having high clinical utility and a production method therefor. The present invention further provides: a lactoferrin fusion protein that retains the biological activity of native lactoferrin while having a significantly extended in vivo life span, and that has more clinical utility than native lactoferrin and recombinant lactoferrin; and a production method therefor. With this fusion protein or a variant thereof, the ability of lactoferrin to bind iron is retained, and therefore at least the important biological activity of lactoferrin that is based on the iron-binding ability is retained. Additionally, this fusion protein or variant thereof has bioavailability and resistance to protease, and thus can exhibit biological activity in vivo over a long period. Furthermore, this fusion protein is not easily broken down by pepsin in the stomach.