Vitamin K-dependent carboxylase: partial purification of the enzyme by antibody affinity techniques.
The vitamin K-dependent carboxylase activity of bovine liver microsomes has been purified 500-fold by adsorption to an antiprothrombin column and elution with a dodeca peptide which competes with a prothrombin precursor enzyme recognition site. The purified enzyme is devoid of bound precursors, and has the same ratio of vitamin K epoxidase activity to carboxylase activity as the crude microsomal preparation.
Harbeck
M C
MC
Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin-Madison 53706.
Cheung
A Y
AY
Suttie
J W
JW
D000818:Animals; D000915:Antibody Affinity; D019735:Carbon-Carbon Ligases; D002417:Cattle; D002846:Chromatography, Affinity; D008025:Ligases / Q000276:immunology / Q000302:isolation & purification*; D008862:Microsomes, Liver / Q000201:enzymology; D006899:Mixed Function Oxygenases / Q000378:metabolism; D011516:Prothrombin / Q000037:antagonists & inhibitors; D064417:Vitamin K Epoxide Reductases
D011516:Prothrombin; D006899:Mixed Function Oxygenases; D064417:Vitamin K Epoxide Reductases; D008025:Ligases; D019735:Carbon-Carbon Ligases; C020660:glutamyl carboxylase