Portal de Periódicos da CAPES

[25] Role of propeptide in vitamin K-dependent γ-carboxylation

1993; Academic Press; Linguagem: Inglês

10.1016/0076-6879(93)22028-e

1557-7988

Karen Kotkow, David A. Roth, Thomas J. Porter, B Furie, B Furie,

Atrial Fibrillation Management and Outcomes

This chapter focuses on the role of propeptide in vitamin K-dependent γ-carboxylation. The vitamin K-dependent coagulation proteins are zymogens, which must be enzymatically cleaved to generate active serine proteases. Several structural domains distinct from the serine protease domain of these proteins are responsible for membrane interaction and protein complex formation. The amino-terminal domain of the vitamin K-dependent proteins is rich in γ-carboxyglutamic acid residues. This amino acid modification confers metal-binding properties, which induce a conformational transition in these proteins. The calcium-stabilized conformer of the vitamin K-dependent proteins binds membrane surfaces. The chapter describes methods for the expression and isolation of recombinant vitamin K-dependent proteins. The method of determining the γ-carboxyglutamic acid content of vitamin K-dependent protein samples is a modification of the method developed by Kuwada and Katayama. This technique is simple and sensitive, allowing determination of the γ-carboxyglutamic acid of picomoles of sample.