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Two experiments were conducted to determine optimal standardized ileal digestible (SID) tryptophan:lysine ratio for piglets using growth performance and plasma urea N as response criteria. In Experiment 1, piglets were fed 6 diets with 8.5, 9.5, 10.5, 11.5, 12.5 or 13.5 g · kg–1 SID lysine to estimate lysine requirement. In Experiment 2, piglets were fed 6 diets with 9.2 g · kg–1 SID lysine, and 0.178, 0.182, 0.196, 0.216, 0.227 or 0.236 SID trytophan:lysine to estimate optimal tryptophan:lysine ratio. The SID lysine requirement was estimated to be 10.2 g · kg–1. Response criteria measured were unaffected by SID tryptophan:lysine ratio, implying that the diets fed were not deficient in tryptophan. In conclusion, the SID lysine requirement for the piglets was close to the recommendation by NRC (1998; 10.1 g · kg–1), but not NRC (2012; 12.3 g · kg–1). The optimal SID tryptophan:lysine ratio of the piglets was either equal to or less than 0.178.
The aim of the study was to determine influence of oxidation degree on available lysine content and protein digestibility in meat products with added antioxidants (rosemary extracts, soy protein hydrolyzate, BHT) stored under frozen conditions.
We have previously reported on the identification and characterization of the Porphyromonas gingivalis A7436 strain outer membrane receptor HmuR, which is involved in the acquisition of hemin and hemoglobin. We demonstrated that HmuR interacts with the lysine- (Kgp) and arginine- (HRgpA) specific proteases (gingipains) and that Kgp and HRgpA can bind and degrade hemoglobin. Here, we report on the physiological significance of the HmuR-Kgp complex in heme utilization in P. gingivalis through the construction and characterization of a defined kgp mutant and a hmuR kgp double mutant in P. gingivalis A7436. The P. gingivalis kgp mutant ex­hibited a decreased ability to bind both hemin and hemoglobin. Growth of this strain with hemoglobin was delayed and its ability to utilize hemin as a sole iron source was diminished as compared to the wild type strain. Inactivation of both the hmuR and kgp genes resulted in further decreased ability of P. gingivalis to bind hemoglobin and hemin, as well as diminished ability to utilize either hemin or hemoglobin as a sole iron source. Collectively, these in vivo results further confirmed that both HmuR and Kgp are involved in the utilization of hemin and hemoglobin in P. gingivalis A7436.
The aim of the study was to determine the influence of oxidation degree on available lysine and methionine content and protein digestibility in meat products with added antioxidants (rosemary extracts, green tea extracts, BHT) stored under frozen conditions. Oxidation degree of lipid using peroxide value (PV), anisidine value (AV), thiobarbituric acid reactive substances (TBARS), and Totox coefficient was controlled and protein digestibility and content of available lysine and methionine were determined periodically. Results showed an increase in lipid oxidation during storage. The highest values for the applied measurement of oxidation were observed in the control sample without antioxidants. The added antioxidants slowed down lipid oxidation to a significant extent. In control samples, the content of available lysine and methionine was reduced by 53% and 75% respectively, whereas protein digestibility by 12.5% at the end of storage. Inhibition of lipid oxidation products formation by the addition of antioxidants, limited significantly lysine and methionine losses and reduction of protein digestibility. The application of antioxidants extended stability and protected biological protein value of the meat products examined.
Usefulness of analytical method (bromocresole purple index – BCPI) as a new and fast way for available lysine (LA) content determination in micro-waved soybean seeds was tested. Due to a great interdependence of LA and BCPI determinations, which was confirmed by high correlation and determination coefficients values (r = 0.78 and R2) for proposed regression equations LA = f(BCPI), the BCPI method appeared to be useful for the description of available lysine (LA) content changes in micro-waved soybean seeds and soybean meal.
Badania przeprowadzono na 2 grupach indorów typu Big-6 podczas 16-tygodniowego odchowu. Czynnikiem doświadczalnym był dodatek miedzi w formie chelatu z lizyną w ilości 10 mg Cu-dm-3H2O. Celem badań było określenie wpływu miedzi jako dodatku do wody pitnej na masę ciała oraz kumulację składników mineralnych w wybranych tkankach indyków. Wykazano, że dodatek chelatu spowodował zwiększenie końcowej masy ciała indorów, natomiast nie wpłynął w znaczący sposób na masę analizowanych tkanek. Stwierdzono, że zastosowanie Cu wpłynęło na wzrost zawartości Cu, Zn i Fe we wszystkich badanych tkankach. Największą retencję Cu wykazano w przypadku wątroby, natomiast najmniejsze ilości tego pierwiastka kumulowały się w mięśniach piersiowych ptaków. Długotrwała aplikacja miedzi nie spowodowała nadmiernej kumulacji tego składnika w nerkach i mięśniach indyków, co nie stanowiło zagrożenia dla zdrowia konsumentów, gdyż jej zawartość nie przekraczała dopuszczalnych norm (5 mg-kg-1; wg PN-A-86524:1994).
The aim of the study was to determine the effect of the addition of antioxidants on changes in contents of available lysine and methionine in raw Polish sausage. Experimental material consisted of four variants of experimental sausages. One variant consisted of a sample with no antioxidant added (control), while the following were added to the other variants: BHT (0.02%), rosemary ethanol extract (0.05%) and soy protein hydrolysate (2%). Oxidation degree of lipid using peroxide value (PV), anisidine value (AV), thiobarbituric acid reactive substances (TBARS) and the Totox index was controlled and content of available lysine and methionine were determined periodically. In order to determine the effect of the addition of antioxidants on the stability of available lysine and methionine, values of the coefficient of the slope of curve of changes in time (coefficient a/24 h) were analyzed along with the half-life period of the amino acids (TIC50). Antioxidants exhibited an inhibitory effect on the advancement of lipid autoxidation reactions and reduced quantitative losses of available lysine and methionine in analyzed sausages. Natural antioxidants exhibited a lower capacity to reduce losses of nutritive value of protein than it was found for BHT.
Chemical modification of arginine and lysine residues of bovine heart 2-oxoglutarate dehydrogenase with phenylglyoxal and pyridoxal 5'-phosphate inactivated the enzyme, indicating the importance of these residues for the catalysis. Inactivation caused by pyridoxal 5'-phosphate was prevented in the presence of thiamine pyrophosphate and Mg2+ allowing the assumption that lysine residues participate in binding of the cofactor.
The active site lysine residue, K256, involved in Schiff's base linkage with pyridoxal-5'-phosphate (PLP) in sheep liver recombinant serine hydroxymethyltransferase (rSHMT) was changed to glutamine or arginine by site-directed mutagenesis. The purified K256Q and K256R SHMTs had less than 0.1% of catalytic activity with serine and H4folate as substrates compared to rSHMT. The mutant enzymes also failed to exhibit the characteristic visible absorbance spectrum (lambda(max) 425 nm) and did not produce the quinonoid intermediate (lambda(max) 495 nm) upon the addition of glycine and H4folate. The mutant enzymes were unable to catalyze aldol cleavage of beta-phenylserine and transamination of D-alanine. These results suggested that the mutation of the lysine had resulted in the inability of the enzyme to bind to the cofactor. Therefore, the K256Q SHMT was isolated as a dimer and the K256R SHMT as a mixture of dimers and tetramers which were converted to dimers slowly. On the other hand, rSHMT was stable as a tetramer for several months, further confirming the role of PLP in maintenance of oligomeric structure. The mutant enzymes also failed to exhibit the increased thermal stability upon the addition of serine, normally observed with rSHMT. The enhanced thermal stability has been attributed to a change in conformation of the enzyme from open to closed form leading to reaction specificity. The mutant enzymes were unable to undergo this conformational change probably because of the absence of bound cofactor.
Four low molecular mass lysine dendrimers were synthesized by Boc chemistry in solution (155 and 169) and Fmoc chemistry on solid support (P2 and P13). The structure and fragmentation mode of the above dendrimers was investigated in gas phase by the LSI-MS and ESI-MS techniques. 1H and 13C NMR analysis in solution (d6-DMSO) allowed to confirm the correct structure. Antimicrobial activities of the dendrimers against Staphylococcus aureus, Escherichia coli and Candida albicans confirmed our hypothesis that the dendrimer structure can be used for construction of molecules interacting with biological membranes.
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