'We're glad that many people are interested to visit us and learn from our experiences,' said Komang Ruditha, Head of TPST 3R Seminyak.
Komang Ruditha and his team of TPST 3R Seminyak started it small in 2004 with 1 mini truck, 3 employees, and 85 customers.
Tyrosine sulfation is a post-translational modification occasionally found in peptides and proteins synthesized through the secretory pathway both in plants and animals.56) A specific enzyme involved in this modification was first identified in mice and humans and named tyrosylprotein sulfotransferase (TPST).
In general, TPST catalyzes the transfer of a sulfate from a donor 3'-phosphoadenosine 5'-phosphosulfate to the phenolic group of tyrosine within the acceptor peptide by forming an enzyme-substrate ternary complex (Fig.
Another chance for affinity purification of TPST arose from the identification of PSY1, the second tyrosine-sulfated peptide in plants.
Arabidopsis TPST (AtTPST) was identified to be a 62-kD transmembrane protein localized in the cis- Golgi.11) As we hypothesized, AtTPST showed no sequence similarity with animal TPST and, more surprisingly, was a type I membrane protein, which has a transmembrane domain near the C-terminus and a large luminal catalytic domain toward the N-terminus, the opposite topological orientation compared with animal TPST.
Making use of our experience in the purification of TPST, we purified HPAT from solubilized Arabidopsis membrane fractions by affinity chromatography and identified 42 kD Golgi-localized type II transmembrane proteins that contained a single transmembrane domain near the N-terminus.