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Plasmepsin-like Aspartyl Proteases in .
Pathogens
September 2021
Institute of Parasitology, Biology Centre, Academy of Sciences of the Czech Republic, Branišovská 1160/31, CZ-37005 České Budějovice, Czech Republic.
Apicomplexan genomes encode multiple pepsin-family aspartyl proteases (APs) that phylogenetically cluster to six independent clades (A to F). Such diversification has been powered by the function-driven evolution of the ancestral apicomplexan AP gene and is associated with the adaptation of various apicomplexan species to different strategies of host infection and transmission through various invertebrate vectors. To estimate the potential roles of APs, we performed qRT-PCR-based expressional profiling of APs (BmASP2, 3, 5, 6), which revealed the dynamically changing mRNA levels and indicated the specific roles of individual BmASP isoenzymes throughout the life cycle of this parasite.
View Article and Find Full Text PDFDiverse activities and biochemical properties of amylase and proteases from six freshwater fish species.
Sci Rep
March 2021
Department of Biochemistry, Faculty of Science, Khon Kaen University, Khon Kaen, 40002, Thailand.
This study investigated the biochemical properties, enzyme activities, isoenzyme pattern, and molecular weight of three types of digestive enzyme from six freshwater fish species: Puntius gonionotus (common silver barb), Puntioplites proctozysron (Smith's barb), Oreochromis niloticus (Nile tilapia), Hemibagrus spilopterus (yellow mystus), Ompok bimaculatus (butter catfish), and Kryptopterus geminus (sheatfish). The optimum pHs for amylase and alkaline protease activities were 7.0-8.
View Article and Find Full Text PDFIdentification of Placental Aspartic Proteinase in the Eurasian Beaver ( L.).
Int J Mol Sci
April 2018
Department of Animal Anatomy and Physiology, Faculty of Biology and Biotechnology, University of Warmia and Mazury in Olsztyn, 10-719 Olsztyn, Poland.
Aspartic proteinases (AP) form a multigenic group widely distributed in various organisms and includes pepsins (pep), cathepsins D and E, pregnancy associated glycoproteins (PAGs) as well as plant, fungal, and retroviral proteinases. This study describes the transcript identification and expression localization of the AP within the discoid placenta of the . We identified 1257 bp of the cDNA sequence, encoding 391 amino acids (aa) of the polypeptide precursor composed of 16 aa signal peptide, 46 aa pro-piece, and 329 aa of the mature protein.
View Article and Find Full Text PDFPartial characterization of digestive proteases in tropical gar Atractosteus tropicus juveniles.
Fish Physiol Biochem
August 2014
Laboratorio de Acuicultura Tropical, División Académica de Ciencias Biológicas, Universidad Juárez Autónoma de Tabasco (UJAT), 0.5 km Carretera Villahermosa-Cárdenas, 86000, Villahermosa, Tabasco, Mexico.
Tropical gar (Atractosteus tropicus) is an economically and socially important freshwater species from Southeastern Mexico, with a high aquaculture potential. With this in mind, the purpose of this study was to characterize the digestive proteases of tropical gar juveniles through biochemical and electrophoretic analyses. Twenty specimens with an average weight of 73.
View Article and Find Full Text PDFPeptide inhibitor modified magnetic particles for pepsin separation.
J Sep Sci
June 2009
Institute of Pathophysiology and Center of Experimental Hematology, First Faculty of Medicine, Charles University in Prague, Czech Republic.
Synthetic heptapeptide containing D-amino acid residues (Val-D-Leu-Pro-Phe-Phe-Val-D-Leu) was coupled to glyoxal-activated magnetic agarose particles via the free peptide amino group. The peptide-modified magnetic particles were used for the separation of pepsins. Porcine pepsin A and human pepsin A were adsorbed to the magnetic peptide-modified affinity carrier, while the rat pepsin C and human pepsin C did not interact with the immobilized ligand.
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