Synthesis of two analogs of a cyclic hexapeptide with disulfide bridge corresponding to bovine prothrombin precursor sequence 18-23. Extent of carboxylation by Vitamin K-Dependent carboxylase.
Rich DH, Kawai M, Goodman HL, Suttie JW.
International Journal of Peptide and Protein Research, 18, 41-51 (1081)
Vitamin K-dependent carboxylase: purification of the rat liver microsomal enzyme.
L M Canfield et al.
Archives of biochemistry and biophysics, 202(2), 515-524 (1980-07-01)
Liver microsomes contain a vitamin K and O2-dependent carboxylase that converts peptide-bound glutamyl residues to gamma-carboxyglutamate residues. The peptide Boc-O-phospho-Ser-O-phospho-Ser-Leu-OMe has now been synthesized. This peptide inhibits the carboxylation of endogenous protein precursors by a detergent-solubilized preparation of the carboxylase
The Journal of biological chemistry, 257(24), 15008-15011 (1982-12-25)
The vitamin K-dependent carboxylase extracted from rat liver microsomes by 3-([3-cholamidopropyl] dimethylammoniol)-1-propane sulfonate detergent solution has been partially purified by chromatography on Ultrogel AcA-34 followed by carboxymethyl-Sepharose chromatography and pentapeptide affinity chromatography. The carboxylase appears to be composed of two
The Biochemical journal, 245(1), 251-255 (1987-07-01)
Vitamin K-dependent carboxylase activity has been demonstrated in the crude microsomal fraction of the intima of bovine aortae. The procedure for the isolation of vessel wall carboxylase is a slight modification of the general preparation procedure for tissue microsomes. The
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