Complete coding sequence of human tryptophan hydroxylase

Complete coding sequence of rat tyrosine hydroxylase mRNA.

Several clones specific for tyrosine hydroxylase [tyrosine 3-monooxygenase, L-tyrosine, tetrahydropteridine:oxygen oxidoreductase (3-hydroxylating), EC 1.14.16.2] have been identified from a rat PC12 library by using the previously characterized clone pTH-1. The most complete of these, pTH-51, is 1758 base pairs long and covers most of the length of the mRNA, including the entire coding and 3' ...

Sequence of two mRNAs encoding active rat tryptophan hydroxylase.

Two full-length cDNA clones that encode functional rat tryptophan hydroxylase (EC 1.14.16.4), the key enzyme in serotonin synthesis, have been isolated from a rat pineal gland library. These two clones correspond to the 1.8- and 4-kilobase mRNA species, respectively. They contain the same coding sequence corresponding to a 51,010-dalton protein and differ in the length of their 3' untranslated ...

Phenylalanine Hydroxylase, Tyrosine Hydroxylase, and Tryptophan Hydroxylase

Production of Recombinant Bacmid Containing the Coding Sequence of Human Hepcidin

Abstract Background and objective: Hepcidin is a cystein-rich antimicrobial peptide, which is secreted by the liver. It fights against wide spectrum of bacteria, viruses and fungi and it is a major regulator of iron homeostasis. Today, scientists have made many efforts on the production of hepcidin. Baculovirus expression system is one of the best eukaryotic expression systems for production of...

High-level expression and deletion mutagenesis of human tryptophan hydroxylase.

Human tryptophan hydroxylase has been expressed as a soluble and active form in Escherichia coli by fusion with an affinity tag, maltose-binding protein. The fusion protein has been purified to near homogeneity by affinity chromatography on crosslinked amylose resin. The purified fusion protein has a specific activity of 86 nmol of 5-hydroxytryptophan per min per mg of fusion protein. A series ...