pLIF has 84% and 86% amino acid sequence identity to mouse and human LIFs, respectively. The deduced amino acid sequence of pLIF protein contains six conserved consensus N-linkedglycosylation sites and six cysteines to form potential disulfide bonds.
Acidohermophlic alpha-amylase BD5063 is found in Thermococcus sp.. The encoding gene BD5063 was reconstructed for the optimal expression in P. pastoris.
ResultsIt is shown through molecular cloning and sequen cing that the coding gene has 507 bp and codes for 168 amino acids. There are gene sequence coding signal peptide,transmembrane and intracellular regions. It also has 3 potential N linked glycosylation sites.
The full length cDNA sequence was 1050 bp with a short 5′ end and long 3′ end untranslated regions,which encoded for 349 amino acids and contained the signal peptide,extracellular region with 3 Ig like domains,transmembrane and intracytoplasmic domain.
Our results suggest that the distinct properties of DNase I exhibited by the three types may be attributed to differences in the extent of post-translational N-linked glycosylation of the enzyme.
Analysis of the deduced amino acid sequence indicated that SPV2 has its core arginine residue, a potential N-linked glycosylation site near its N-terminal, and one transmembrane domain in its C-terminal.
N-linked glycosylation occurs co-translationally and plays a role in the maturation and processing of the receptor, while palmitoylation is involved in receptor endocytosis and post-endocytic trafficking.
The human IL-3 gene encodes a protein of 133 amino acids with two conserved cysteine residues and 2 potential N-linked glycosylation sites; human native IL-3 has not been characterized.
The predicted CbICE53 protein contained a potential basic helix-loop-helix domain, a nuclear localization signal (NLS), an RNA-binding region (RGG box), and N-glycosylation and kinase phosphorylation sites.
The lectin activity of one of the recombinant B chains was close to that of the native protein, which was attributed to the lack of N-glycosylation sites in the latter.
This suggestion is based on the discovery in the genome of the human microsporidian Encephalitozoon cuniculi of three genes responsible for the O-mannosylation of proteins with a lack of enzymes participating in N-glycosylation.