PREPARATIVE PURIFICATION PROCESS FOR HUMAN FURIN

Recombinant truncated human furin was expressed in CHO cells and concentrated approximately 50 -fold by ultrafiltration and diafiltration. The concentrate was purified by column chromatography on Capto-MMC„¢ resulting in a 30-50 fold purification factor and a yield of at least 60%. The at least 20%...

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Bibliographic Details
Main Authors ROMEDER-FINGER, STEFAN, TURECEK, PETER, SCHWARZ, HANS-PETER, MATTHIESSEN, PETER
Format Patent
LanguageCroatian
English
Published 31.07.2013
Subjects
BEER
BIOCHEMISTRY
CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOIDCHEMISTRY
CHEMISTRY
COMPOSITIONS THEREOF
CULTURE MEDIA
ENZYMOLOGY
HUMAN NECESSITIES
HYGIENE
MEDICAL OR VETERINARY SCIENCE
METALLURGY
MICROBIOLOGY
MICROORGANISMS OR ENZYMES
MUTATION OR GENETIC ENGINEERING
ORGANIC CHEMISTRY
PEPTIDES
PERFORMING OPERATIONS
PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
PROPAGATING, PRESERVING OR MAINTAINING MICROORGANISMS
SEPARATION
SPIRITS
THEIR RELEVANT APPARATUS
TRANSPORTING
VINEGAR
WINE
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Summary:Recombinant truncated human furin was expressed in CHO cells and concentrated approximately 50 -fold by ultrafiltration and diafiltration. The concentrate was purified by column chromatography on Capto-MMC„¢ resulting in a 30-50 fold purification factor and a yield of at least 60%. The at least 20% pure preparation obtained after Capto-MMC„¢ chromatography had already a purification degree allowing on-column maturation of pro-VWF. Then an additional Arginine Sepharose chromatography purification was carried out. This two column process for purification of truncated human furin resulted in an almost pure furin preparation with a specific activity of approximately 290,000 U furin/mg protein and a yield of about 50%.
Bibliography:Application Number: HR2013P000560T