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1.
Fish Physiol Biochem ; 46(1): 145-155, 2020 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-31707568

RESUMO

Trypsin gene (try) expression levels were quantified in different organs of wild and captive tropical gar (Atractosteus tropicus) adults, and changes in expression during initial ontogeny of the species were determined. RNA was extracted from the pancreas, and cDNA was synthesized and later amplified by endpoint PCR using oligonucleotides designed from different try sequences of fish registered in GenBank. Subsequently, specific oligonucleotides were designed from the partial sequences. Gene expression was measured after RNA extraction and synthesis of the cDNA of 11 organs (liver, pancreas, stomach, esophagus, intestine, pyloric caeca, brain, muscle, gills, gonad, and kidney) of captive and wild adults. Likewise, samples of A. tropicus larvae were taken on days 0 (embryo), 5, 10, 15, 20, 25, and 30 days after hatching (DAH), the RNA was extracted, and the synthesis of cDNA was carried out to measure real-time gene expression (qPCR). The results showed that the highest relative try expression occurred mainly in the esophagus, liver, stomach, and pancreas of both wild and captive adult fish; however, captive organisms had a higher try expression level than wild fish. Although try expression during initial ontogeny was high in embryos (0 DAH), it did not reach the maximum value until 15 DAH. It was concluded that try expression levels in captive adults are due to the high protein content in the balanced feed (trout diet). The highest try expression level during larviculture was detected at 15 DAH, which indicates that A. tropicus larvae have a mature digestive system and can efficiently hydrolyze proteins from feed at this developmental stage.


Assuntos
Proteínas de Peixes/genética , Peixes/fisiologia , Tripsina/genética , Animais , Expressão Gênica
2.
3 Biotech ; 8(4): 186, 2018 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-29556440

RESUMO

In fishes, trypsins are adapted to different environmental conditions, and the biochemical and kinetic properties of a broad variety of native isoforms have been studied. Proteolytic enzymes remain in high demand in the detergent, food, and feed industries; however, our analysis of the literature showed that, in the last decade, some fish trypsins have been studied for the synthesis of industrial peptides and for specific biomedical uses as antipathogenic agents against viruses and bacteria, which have been recently patented. In addition, innovative strategies of trypsin administration have been studied to ensure that trypsins retain their properties until they exert their action. Biomedical uses require the production of high-quality enzymes. In this context, the production of recombinant trypsins is an alternative. For this purpose, E. coli-based systems have been tested for the production of fish trypsins; however, P. pastoris-based systems also seem to show great potential in the production of fish trypsins with higher production quality. On the other hand, there is a lack of information regarding the specific structures, biochemical and kinetic properties, and characteristics of trypsins produced using heterologous systems. This review describes the potential uses of fish trypsins in biomedicine and the enzymatic and structural properties of native and recombinant fish trypsins obtained to date, outlining some prospects for their study.

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