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Purification and characterization of osteopontin from human milk

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Osteopontin (OPN) is expressed in many organs and tissues and has different biological properties related to different molecular forms in respect to size and posttranslational modifications. However, a purification procedure for authentic intact OPN as well as fragments of OPN from an accessible biological source is missing. A four-step procedure was used to purify OPN from human milk, based on its crystal growth inhibitory activity, including anion exchange chromatography, the elimination of casein, hydroxyapatite chromatography, and negative affinity chromatography. Purified OPN was further separated into its different molecular forms by means of a two-step procedure, involving size exclusion chromatography and reverse phase chromatography. A rabbit polyclonal antibody was raised to purified intact OPN and high M(r) OPN components; the immunoreactivity of both forms was almost equal when investigated by enzyme immunoassay (EIA). The procedures facilitate the purification of intact OPN and OPN fragments for purposes of standardization, preparation of monospecific antibodies, and functional studies.
Bidragets oversatte titelPurification and characterization of osteopontin from human milk.
OriginalsprogEngelsk
TidsskriftProtein Expression and Purification
Vol/bind30
Udgave nummer2
Sider (fra-til)238-245
Antal sider8
ISSN1046-5928
StatusUdgivet - 2003

ID: 32550921