Identification of the N-Terminal Heparin Binding Site of Rat Tyrosine Hydroxylase
Abstract
The first step in catecholamine biosynthesis is the hydroxylation of tyrosine to form dihydroxyphenylalanine (DOPA). This step is rate-limiting and is catalyzed by the enzyme tyrosine hydroxylase. This enzyme binds heparin at some point in the amino terminal domain, the first 155 amino acid residues. In order to further elucidate the binding site of heparin, successive N-terminal truncates were made, and experiments were done to analyze the binding of those truncates to heparin. We found the heparin binding site to be possibly located in the first 85 amino acid residues of the protein.
Description
Program year: 1996/1997Digitized from print original stored in HDR
Citation
Spencer, M. Michelle (1994). Identification of the N-Terminal Heparin Binding Site of Rat Tyrosine Hydroxylase. University Undergraduate Fellow. Available electronically from https : / /hdl .handle .net /1969 .1 /CAPSTONE -SpencerM _1994.