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| Martinez-Pacheco,Mauro Manuel; Flores-Garcia,Alberto; Venegas-Gonzalez,Eulalio; Cepeda-Villegas,Mario Alberto. |
| Hybrids of Zea mays L. (Buffalo, Falcon, H360 y HV313) were treated with citric acid (2000 ppm). Grain yield, soluble protein and proteolytic activity were monitored when the crop reached physiological maturity. Citric acid was applied before the appearance of the flag leaf, and induced an increase in the grain yield from 4222 to 5780 kg/ha, in the soluble protein from 6.34 to 7.91 mg/mg and into the proteolytic activity from 14.3 to 65.7 µU mg prot-1. This is an increase of 2 to 12 times in the Falcon, H360 and HV313 hybrids, while the Buffalo hybrid responded with less intensity to the treatment with citric acid. In the H360 hybrid treated with citric acid, an increase in the proteolytic activity of aspartyl serine proteases was observed. The results... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Maize; Citric acid; Proteolytic activity. |
| Ano: 2011 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1413-70542011000500007 |
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| LUKIN,Aleksandr. |
| Abstract Protepsin belongs to the class of acid proteinases, containing carboxyl groups in the active center. The preparation cleaves peptide bonds formed by aromatic amino acids (tyrosine, phenylalanine), and does not hydrolize esters and amides. Along with the proteolytic complex, Protepsin contains collagenase, lipase, and other digestive enzymes. The preparation is obtained according to the original technology through maceration of animal endocrine raw materials, followed by purification, concentration, isolation and freeze dehydration of the enzyme complex. The results of the laboratory studies of the proteolytic activity of enzyme preparations show that Protepsin, the preparation of animal origin with a proteolytic activity of 100 units/g, has the... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Enzyme preparations; Protepsin; Cattle by-products; Proteolytic activity; Protein hydrolysate. |
| Ano: 2019 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612019005028106 |
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| LIMA,P. R. M. DE; BROCHETTO-BRAGA,M. R.; CHAUD-NETTO,J.. |
| Some properties of a Africanized honeybee venom proteases were determined by enzymatic assays in solution, electrophoresis in SDS-PAGE, and gel filtration. Bee venom extracts were obtained by reservoir disruption, selective dialysis (cut off 12 kDa) to eliminate small components, such as the protease inhibitor present in the venom, and then fractionation of the dialyzed extract by gel filtration on a Sephadex G-100 column. The optimal conditions for the caseinolytic assays were pH 9.5, 2-hour digestion at 37 °C, and 1% casein concentration. The proteolytic activity was also determined by electrophoresis in SDS-PAGE with co-polymerized gelatin with three major bands of 66.0, 41.6, and 25.1 kDa. A principal serine-protease-like mechanism was revealed in the... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Venom; Africanized bee; Apis mellifera; Proteolytic activity; Gel filtration chromatography. |
| Ano: 2000 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0104-79302000000100004 |
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| Campos,Fabiana V.; Menezes,Thiago N.; Malacarne,Pedro F.; Costa,Fábio L. S.; Naumann,Gustavo B.; Gomes,Helena L.; Figueiredo,Suely G.. |
| Abstract The most poisonous fish species found along the Brazilian coast is the spotted scorpionfish Scorpaena plumieri. Though hardly ever life-threatening to humans, envenomation by S. plumieri can be quite hazardous, provoking extreme pain and imposing significant socioeconomic costs, as the victims may require days to weeks to recover from their injuries. In this review we will walk the reader through the biological features that distinguish this species as well as the current epidemiological knowledge related to the envenomation and its consequences. But above all, we will discuss the challenges involved in the biochemical characterization of the S. plumieri venom and its compounds, focusing then on the successful isolation and pharmacological... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Scorpionfish; Scorpaena plumieri venom; Inflammatory response; Proteolytic activity; Cardiovascular activity; Sp-GP; Plumieribetin; C-type lectins; Sp-CTx. |
| Ano: 2016 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992016000100205 |
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