We investigated nutritional characteristics and active components in the liver of Wagyu×Qinchuan cattle and Qinchuan cattle produced in Shaanxi (China). We observed significant differences (p<0.05) in the proximate composition of protein, fat, carbohydrate, total energy, and glycogen. Wagyu×Qinchuan cattle liver showed higher (p<0.05) sodium, iron, zinc, and selenium concentrations than Qinchuan cattle liver. The amino acid composition of Wagyu×Qinchuan cattle liver was richer (p<0.05) in 13 types of amino acids, with the exception of Asp (10.06%), Val (5.86%), and Met (1.72%). Total essential amino acids accounted for almost half the composition (39.69%) in Wagyu×Qinchuan cattle liver. Wagyu×Qinchuan cattle liver had lower (p<0.05) levels of monounsaturated fatty acids (18.2%), but higher (p<0.05) levels of polyunsaturated fatty acids (35.11%), compared with Qinchuan cattle liver (23.29% and 28.11%, respectively). The thrombogenic index was higher in Qinchuan cattle liver (0.86) than in Wagyu×Qinchuan cattle liver (0.70), and the glutathione (38.0 mg/100g) and L-carnitine (2.12 μM/g) content was higher (p<0.05) in Wagyu×Qinchuan cattle liver than in Qinchuan cattle liver (29.8 mg/100g and 1.41 μM/g, respectively). According to the results obtained, the liver of Wagyu×Qinchuan cattle, which is insufficiently used, should be increasingly utilized to improve its commercial value.
N-Glycosylation is a common form of protein post-translational modification in Pichia pastoris and greatly affects folding and secretion. The propeptide of the Pseudomonas aeruginosa elastase (PAE) is indispensable for proper folding and secretion of the enzyme. We have studied the effect of introducing N-glycosylation sites to the propeptide of the recombinant elastase (rPAE) on its expression levels in P. pastoris. Addition of N-glycosylation sites to the propeptide at N51 or N93 enhanced rPAE production levels by 104 or 57%, respectively, while addition at N11 or N127 led to a 25 or 50% decrease, respectively. The introduced N-glycosylation sites in the propeptide at these four sites exerted a null effect on the N-glycosylation degree of mature rPAE.
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