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Overall, low caloric intake was associated with a more negative protein balance compared with high caloric intake.
In the patient group studied, hypocaloric feeding was associated with a more negative protein balance, but the amino acid oxidation was not different.
Hypocaloric feeding was found to be associated with a more negative protein balance, but with unaltered amino acid oxidation, compared to normocaloric feeding.
In the critically ill neurosurgical patients treated in the ICU, hypocaloric feeding was associated with a more negative protein balance, while the amino acid oxidation was not different.
Whole-body protein synthesis was lower during hypocaloric feeding while whole-body protein degradation was unaltered, which resulted in a more negative protein balance (-1.9 ± 2.1 vs. -0.7 ± 1.3 mg phenylalanine/kg/hour, p = 0.014).
The phenylalanine tracer indicated that whole-body protein synthesis was lower during hypocaloric feeding, while whole-body protein degradation and amino acid oxidation were unaltered, which resulted in a more negative protein balance, namely −1.9 ± 2.1 versus −0.7 ± 1.3 mg phenylalanine/kg/h (P = 0.014).
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Broadly speaking, these were (EPC1) from long, polar, high-O content proteins to aromatic, high-C proteins; (EPC2) from hydrophobic, high-GC proteins to positive, high-N proteins, (EPC3) from more polar proteins to more negative, more hydrophobic proteins and (EPC4) from GC-poor, S-rich, aromatic proteins to GC-rich, positively charged proteins.
Carrying one more negative charge than untagged protein, the paramagnetically tagged ZFD protein was purified with Source-Q chromatography, and was confirmed by ESI-MS (Bruker Daltonics, Billerica MA).
At low temperatures, the far-UV CD spectrum of RIα 92 381) resembled that of RIα, whether recorded in the absence or presence of cAMP, but the ellipticity values after denaturation at high temperatures were markedly more negative for the truncated protein relative to full-length protein (Figure 2A).
Our report described a novel strategy on this protein by replacing nonpotential aminoacids influencing the biological activity of the protein with more negative aminoacid, hence increasing the net negative charge of the protein.
Many of the ALS-associated point mutations in SOD1 reduce the net negative charge of SOD1; however, three ALS mutants would be expected to possess a protein charge more negative than WT SOD1 (Fig. 3, Table 1).
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more negative content
more organic protein
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more animal protein
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more basic protein
more negative potential
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