Evidence for the glycoprotein nature of vitamin K-dependent carboxylase from rat liver.
The ability of the rat liver microsomal vitamin K-dependent carboxylase and microsomal precursors of prothrombin and other vitamin K-dependent proteins to bind to lectin gels has been determined. Under denaturing conditions which dissociate precursor substrates from the carboxylase enzyme, prothrombin precursors and microsomal proteins labeled in gamma-carboxyglutamate residues with [14C]bicarbonate were nearly quantitatively bound to concanavalin A gels. When lentil lectin gels were used, only about one third of these proteins were bound, suggesting a heterogeneity of this glycoprotein pool. Under non-denaturing conditions, both precursor proteins and vitamin K-dependent carboxylase activity were retained on either concanavalin A or lentil lectin gels. These data are consistent with an increase in lectin binding determinants in the precursor-carboxylase complex and are evidence for the glycoprotein nature of this microsomal enzyme.
D000818:Animals; D001639:Bicarbonates / Q000378:metabolism; D019735:Carbon-Carbon Ligases; D002845:Chromatography; D003208:Concanavalin A / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism*; D037102:Lectins / Q000378:metabolism*; D008025:Ligases / Q000378:metabolism*; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D037121:Plant Lectins; D011498:Protein Precursors / Q000378:metabolism; D011516:Prothrombin / Q000378:metabolism; D051381:Rats
D001639:Bicarbonates; D006023:Glycoproteins; D037102:Lectins; D037121:Plant Lectins; D011498:Protein Precursors; C033619:lentil lectin; D003208:Concanavalin A; D011516:Prothrombin; D008025:Ligases; D019735:Carbon-Carbon Ligases; C020660:glutamyl carboxylase