For the first time, an analysis was carried out of allozyme variability in trout (Salmo trutta) from three rivers of Iran. We studied 23 gene loci coding enzymes: glycerol-3-phosphate dehydrogenase (G3PDH), aspartate aminotransferase (AAT), malate dehydrogenase (MDH), lactate dehydrogenase (LDH), creatine kinase (CK), malic enzyme [NADP-dependent MDH] (MEP), superoxide dismutase (SOD), esterase (EST), and esterase D (EST-D). The obtained data demonstrate the similarity between the trout samples from different rivers of Iran according to genetic characteristics. Taking into account the differences by allozyme markers of allele frequencies and allele composition of some loci, we should expect that Iranian trout diverges significantly in genetics from the other trout populations of the Caspian Sea.
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http://dx.doi.org/10.1186/2193-1801-1-48 | DOI Listing |
Fish Physiol Biochem
January 2025
Institute of Agrifood Research and Technology (IRTA), Centre de La Ràpita, Crta. Poble Nou del Delta Km 5.5, 43540, la Ràpita, Spain.
The effect of different feeding habits on gut morphology and digestive function has been intensively studied during the last decades but sympatric closely related fishes are relatively rare objects of such studies. In the present study, we have identified both morphological and physiological changes in the digestive system of a sympatric pair of whitefish represented by "normal" Coregonus lavaretus pidschian (benthivorous) and "dwarf" C. l.
View Article and Find Full Text PDFFront Bioeng Biotechnol
October 2024
Large Molecule Research, Roche Pharma Research and Early Development (pRED), Roche Innovation Center Munich, Penzberg, Germany.
We present a detailed mass spectrometric analysis of three 2 + 1 T-cell bispecific monoclonal antibodies (TCB mAbs), where an unexpected +15.9950 Da mass shift in tryptic peptides was observed. This modification was attributed to the occurrence of 5R-hydroxylysine (Hyl) using a hybrid LC-MS/MS molecular characterization and CRISPR/Cas9 gene deletion approach.
View Article and Find Full Text PDFStructure
November 2024
Department of Chemistry, Faculty of Science, University of South Bohemia in České Budějovice, Branišovská 1760, CZ-37005 České Budějovice, Czech Republic. Electronic address:
β-Galactosidase from Bacillus circulans ATCC 31382 (BgaD) is a biotechnologically important enzyme for the synthesis of β-galactooligosaccharides (GOS). Among its four isoforms, isoform A (BgaD-A) has distinct synthetic properties. Here, we present cryoelectron microscopy (cryo-EM) structures of BgaD-A and compare them with the known X-ray crystal structure of isoform D (BgaD-D), revealing substantial structural divergences between the two isoforms.
View Article and Find Full Text PDFInt J Mol Sci
September 2024
Department of Endocrinology and Metabolism, Amsterdam Gastroenterology Endocrinology Metabolism, Amsterdam UMC Location University of Amsterdam, 1105 AZ Amsterdam, The Netherlands.
J Inherit Metab Dis
September 2024
Department of Cardiovascular Medicine, First Faculty of Medicine, Charles University, Prague, Czech Republic.
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