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Purification and characterization of the alpha form of rat plasma kallikrein.
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1987
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Protein ChemistrySerine Proteinase GlycoproteinProtein FunctionGlycosylationBiochemistryAlpha FormMedicineBioanalysisGlycobiologyRat Plasma KallikreinBovine KallikreinsPharmacologyProtein PhosphorylationChromatographyProtein Purification
A four-step procedure was used to purify rat plasma kallikrein (RPK) with a relative molecular mass (Mr) of 87 kD (obtained both by gel filtration and SDS-PAGE), which indicates the purification of an alpha (intact) kallikrein, in contrast to previously described RPK preparations which had lower Mr (beta or degraded form). RPK is a neutral (pI 6.7) serine proteinase glycoprotein (15% carbohydrates) and contains (residues/mol): galactose (27), N-acetylglucosamine (24), mannose (13), glucose (13) and fucose (7). This purified alpha form of RPK has properties very similar to those of pure human and bovine kallikreins.