Article
Endoproteolytic processing of the dibasic cleavage site in the human protein C precursor in transfected mammalian cells: effects of sequence alterations on efficiency of cleavage.
Biochemistry - 16 Jan 1990
Foster D C, Sprecher C A, Holly R D, Gambee J E, Walker K M, Kumar A A
Abstract excerpt
The human protein C precursor undergoes extensive co- and posttranslational modification during its biosynthesis in the liver. These modifications include glycosylation, gamma-carboxylation and beta-hydroxylation of specific amino acids, and endoproteolytic processing to remove the pre- and propeptides and also to remove the pair of basic amino acids that connect the light and heavy chains in the precursor....
Topics
- Amino Acid Sequence
- Animals
- Binding Sites
- Cell Line
- Cloning, Molecular
- Cricetinae
- Cyanogen Bromide
- Endopeptidases
- Humans
- Immunosorbent Techniques
- Molecular Sequence Data