Article
Evidence that differentiates between precursor cleavages at dibasic and Arg-X-Lys/Arg-Arg sites.
Journal of biochemistry - 1 Nov 1991
Nagahama M, Ikemizu J, Misumi Y, Ikehara Y, Murakami K, Nakayama K
Abstract excerpt
It is well known that precursor cleavage at paired basic amino acids (e.g., Lys-Arg, Arg-Arg) within the regulated secretory pathway is one of the key steps to produce bioactive peptides. On the other hand, we have recently shown that precursors with an Arg residue at the fourth residue upstream of the cleavage site besides the basic pair, i.e. with the Arg-X-Lys/Arg-Arg (RXK/RR) motif, are cleaved within the...
Topics
- Amino Acid Sequence
- Animals
- Antifungal Agents
- Arginine
- Binding Sites
- Brefeldin A
- CHO Cells
- Calcium
- Colchicine
- Cricetinae
- Cricetulus
- Cyclopentanes