Claim Missing Document
Check
Articles

Found 2 Documents
Search
Journal : Journal of Tropical Life Science : International Journal of Theoretical, Experimental, and Applied Life Sciences

Spatial Distribution and Genetic diversity of Tripneustes gratilla in Ambon Island Veince Benyamin Silahooy; luchman Hakim; Hamid Toha; widodo .
Journal of Tropical Life Science Vol. 3 No. 3 (2013)
Publisher : Journal of Tropical Life Science

Show Abstract | Download Original | Original Source | Check in Google Scholar

Abstract

Tripneustes gratilla an important ecological role in various habitats because T. gratilla is directly or indirectly recycling key from the nutrients in the waters of Ambon Island. Ambon Island has a distinctive topography, thus causing inhibition of water exchange period naturally in Ambon Bay and feared to complicate the exchange of genes between populations thus causing inbreeding. In addition the increasing environmental pollution can narrow the habitat of Tripneustes gratilla. Therefore, this study aims to determine the spatial distribution and genetic diversity of sea urchins (Tripneustes gratilla) on Ambon island based on cytochrome c oxidase subunit 1 gene. Alignment results showed the presence of genetic variation of T. gratilla on the Ambon island. This is shown in several polymorphic base where there has tranversi experience, transition, and insertion. COI gene sequence similarity values of T. gratilla on Ambon island is around 98.4 to 100%. Distribution of T. gratilla population found on Ambon island generally have a relatively small number of individuals. From four locations that just only one location have large enough number of individuals. However, the results of genetic analysis using COI gene showed the presence of genetic closeness between T. gratilla despite located in different locations.
Interaction Of Platelet Activating Factor Acetyl Hydrolase (Paf Ah) Enzyme In Gln281 To Arg281 Mutation Toward Paf And Its Molecular Dynamic Jayarani Fatimah Putri; widodo .; Muhammad Saifur Rohman
Journal of Tropical Life Science Vol. 4 No. 1 (2014)
Publisher : Journal of Tropical Life Science

Show Abstract | Download Original | Original Source | Check in Google Scholar

Abstract

Platelet Activating Factor Acetyl Hydrolase (PAF AH) or LpPLA2 is key enzyme in myocardial infarction catalyzes the sn-2 acetyl group of Platelet Activating Factor (PAF) into lyso PAF and acetate as non-potent inflammatory molecules. PAF AH plays a critical role in arterial plaque development of Coronary Artery Disease (CAD). A crystal structure of PAF AH complexes with other ligand and effects of amino acid alteration to protein plasma consequence have also been reported. Here we report on the result of molecular docking and Molecular dynamic (MD) simulation carried out for PAF AH wild type (WT)/PAF and mutant Q281R/PAF complexes. Docking result shown that amino acid residues on active site of Q281 PAF AH mutant have not recognized on PAF AH. Eelectrostatics and hydrophobic bonds significantly reduced in Q281R than wild type. In the 7500 ps MD simulation Q281R showed less dynamics than WT but enzymatic machinary of mutant Q281R was not interrupted during MD simulation as well as PAF AH wildtype. These findings clearly indicated the importance effect of mutant Q281R in PAF AH recognition to its substrate