scholarly journals Differences and Effects of Metabolic Fate of Individual Amino Acid Loss in High-Efficiency Hemodialysis and Hemodiafiltration

2020 ◽  
Vol 30 (5) ◽  
pp. 440-451 ◽  
Author(s):  
Stefano Murtas ◽  
Roberto Aquilani ◽  
Paolo Iadarola ◽  
M.L. Deiana ◽  
R. Secci ◽  
...  
Agronomy ◽  
2021 ◽  
Vol 11 (2) ◽  
pp. 221
Author(s):  
Elsa Mecha ◽  
Sofia Natalello ◽  
Bruna Carbas ◽  
Andreia Bento da Silva ◽  
Susana T. Leitão ◽  
...  

The common bean (Phaseolus vulgaris L.) represents a sustainable and affordable source of protein, namely, to populations with vegetarian dietary habits. Despite the national germplasm genetic diversity, little is known about the Portuguese accessions’ nutritional and protein quality, leading to their underuse in breeding programs. To fill this gap, a representative collection (106 accessions) was cropped under two contrasting environments (traditional versus heat stress) and evaluated in terms of nutritional quality by near-infrared spectroscopy. Protein quality was assessed, under the stressful environment, considering the individual amino acid contents and the activity of trypsin inhibitors through mass spectrometry (LC-MS/MS) and spectrophotometry, respectively. On top of strong genotypic control, the nutritional composition (protein, fat, fiber, moisture and ash) was also highly influenced by the environment and by genotype × environment interaction, with a clear nutritional quality ranking change for the accessions in heat stress conditions. Classified into three clusters, the accessions from the cluster with the highest individual amino acid and protein contents also showed higher trypsin inhibitor activity (TIA). Since different levels of TIA had no translation into contrasting protein digestibility, breeders focusing on common beans’ protein quality improvement, especially under challenging warming climate conditions, may take advantage of this group of accessions.


1977 ◽  
Vol 26 (7) ◽  
pp. 667-670 ◽  
Author(s):  
C.Richard Truex ◽  
Lena Brattsten ◽  
Willard J. Visek

2002 ◽  
Vol 120 (5) ◽  
pp. 707-722 ◽  
Author(s):  
A.K. Stewart ◽  
M.N. Chernova ◽  
B.E. Shmukler ◽  
S. Wilhelm ◽  
S.L. Alper

We reported recently that regulation by intracellular pH (pHi) of the murine Cl−/HCO3− exchanger AE2 requires amino acid residues 310–347 of the polypeptide's NH2-terminal cytoplasmic domain. We have now identified individual amino acid residues within this region whose integrity is required for regulation of AE2 by pH. 36Cl− efflux from AE2-expressing Xenopus oocytes was monitored during variation of extracellular pH (pHo) with unclamped or clamped pHi, or during variation of pHi at constant pHo. Wild-type AE2–mediated 36Cl− efflux was profoundly inhibited by acid pHo, with a value of pHo(50) = 6.87 ± 0.05, and was stimulated up to 10-fold by the intracellular alkalinization produced by bath removal of the preequilibrated weak acid, butyrate. Systematic hexa-alanine [(A)6]bloc substitutions between aa 312–347 identified the greatest acid shift in pHo(50) value, ∼0.8 pH units in the mutant (A)6342–347, but only a modest acid-shift in the mutant (A)6336–341. Two of the six (A)6 mutants retained normal pHi sensitivity of 36Cl− efflux, whereas the (A)6 mutants 318–323, 336–341, and 342–347 were not stimulated by intracellular alkalinization. We further evaluated the highly conserved region between aa 336–347 by alanine scan and other mutagenesis of single residues. Significant changes in AE2 sensitivity to pHo and to pHi were found independently and in concert. The E346A mutation acid-shifted the pHo(50) value to the same extent whether pHi was unclamped or held constant during variation of pHo. Alanine substitution of the corresponding glutamate residues in the cytoplasmic domains of related AE anion exchanger polypeptides confirmed the general importance of these residues in regulation of anion exchange by pH. Conserved, individual amino acid residues of the AE2 cytoplasmic domain contribute to independent regulation of anion exchange activity by pHo as well as pHi.


1987 ◽  
Vol 67 (4) ◽  
pp. 1143-1148 ◽  
Author(s):  
B. A. CROOKER ◽  
J. H. CLARK ◽  
R. D. SHANKS ◽  
G. C. FAHEY Jr.

Seven feeds were individually incubated (12 h) in ruminally suspended polyester bags. Several alterations (P < 0.05) between individual amino acid compositions of feeds and their respective residues were detected after adjusting for microbial contamination of residues. Detection of diaminopimelic acid in feeds suggests that not all diaminopimelic acid in digesta originates from bacteria. Key words: Amino acid, ruminal degradation, microbial attachment, diaminopimelic acid


1976 ◽  
Vol 22 (5) ◽  
pp. 397-403 ◽  
Author(s):  
Keiichiro MURAMATSU ◽  
Takayuki ARITO ◽  
Hiroshi TSUDA

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