Amino acids in blood plasma and tissues of rats following glucose force-feeding

1969 ◽  
Vol 47 (3) ◽  
pp. 323-327 ◽  
Author(s):  
J. E. Knipfel ◽  
H. G. Botting ◽  
F. J. Noel ◽  
J. M. McLaughlan
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Blood Plasma ◽  
Protein Composition ◽  
Tissue Uptake ◽  
Body Protein ◽  
Glucose Administration ◽  
Force Feeding ◽  
Amino Acid Requirements ◽  
Concentration Changes

Changes in plasma amino acid (PAA) concentrations effected by force-feeding glucose to rats were studied in two experiments. Attempts were made to relate PAA concentration changes to amino acid requirements, previous diet, time after feeding glucose, and composition of several body proteins. Distribution of 14C-lysine between blood and tissues was examined in an additional rat experiment. Previous diet did not affect the relative quantities of amino acids removed from plasma (PAA removal pattern) after glucose force-feeding. Minimal PAA concentrations occurred by 40 min after glucose administration. The PAA removal pattern was not distinctly related to either amino acid requirements or to any particular body protein composition. Results of administering 14C-lysine simultaneously with glucose indicated that decreased plasma 14C-lysine levels were caused by increased tissue uptake of 14C, likely mediated by insulin. Muscle acted as the major recipient of 14C from plasma, with liver a lesser and more dynamic reservoir of 14C accumulation. Work is continuing to further clarify the significance of the PAA removal pattern, caused by the force-feeding of glucose.

Effects of atropine on plasma amino acid profiles and on the synthesis of individual milk proteins in dairy cows fed with pasture

2003 ◽  
Vol 70 (4) ◽  
pp. 373-378 ◽  
Author(s):  
Martin J Auldist ◽  
Catherine M Menzies ◽  
Colin G Prosser
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Blood Plasma ◽  
Latin Square ◽  
Milk Proteins ◽  
Protein Composition ◽  
Essential Amino Acids ◽  
Plasma Amino Acid ◽  
Milk Components ◽  
In Blood Plasma

Effects of atropine on blood plasma amino acid profile and on the yields and concentration of milk components were investigated in 12 Friesian cows in early lactation. Cows were housed indoors and fed with cut pasture ad libitum. Each cow received four treatments over 12 d during a replicated 4×4 Latin square experiment. Treatments were: control (saline); low dose (L; 30 μg atropine/kg body weight (BW)); medium dose (M; 40 μg atropine/kg BW); and 2×L dose, 2 h apart (2×L). On each of four treatment days, cows were milked at about 7.00, after which treatments were administered by subcutaneous injection. Cows were milked again at 2 h, 6 h and 10 h after injection. Milk samples were collected at each milking. Immediately after the 2 h milking, blood samples were drawn from each cow and the second injection was given for the 2×L treatment. Atropine reduced hourly milk yield, and concentrations and hourly yields of total protein, casein, whey protein, α-casein, β-casein, κ-casein, β-lactoglobulin and α-lactalbumin, but by differing amounts. Milk concentrations of bovine serum albumin and immunoglobulin G were increased by atropine, and overall yields of these proteins were mostly unchanged. Atropine lowered concentrations of most, but not all, amino acids in blood plasma, with essential amino acids reduced more than non-essential amino acids. Concentrations of α-amino N in whole blood, and glucose and insulin in blood plasma, fell after atropine injection. There was no difference between the L and M doses of atropine, but the 2×L dose had greater effects on milk composition than the single doses. For yields of milk and milk components, the effect of the 2×L dose was also more persistent. The results highlight the differential synthesis of individual milk proteins, and suggest that atropine might be useful for evaluating the mechanisms regulating milk protein composition.

The tissue and dietary protein and amino acid requirements of pigs from 8.0 to 20.0 kg live weight

1988 ◽  
Vol 46 (2) ◽  
pp. 283-290 ◽  
Author(s):  
R. G. Campbell ◽  
M. R. Taverner ◽  
C. J. Rayner
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Dietary Protein ◽  
Protein Concentration ◽  
Live Weight ◽  
Body Protein ◽  
Digestible Energy ◽  
Protein Deposition ◽  
Amino Acid Requirements ◽  
Ideal Protein

AbstractForty-three entire males were used to determine the pig's tissue requirements for protein and amino acids from 8·0 to 20·0 kg, and provide information on the capacity of diets formulated with conventional ingredients to contain the same levels and balances of amino acids as ideal protein to supply these nutrients. Seven diets with similar digestible energy (15·9 MJ digestible energy (DE) per kg) and crude protein concentrations from 119 to 232 g/kg (8·7 to 17·3 g lysine per kg) were offered ad libitum between 8·0 and 200 kg live weight. The rate of protein deposition was determined by comparative slaughter. The composition of the protein deposited in the whole empty body was determined from amino acid analyses of pigs killed at 8·0 kg and from the two extreme dietary treatments at 20·0 kg. Growth performance and the rates at which protein and lysine were deposited in the empty body increased linearly with increasing dietary protein concentration up to 187 g/kg and remained relatively constant thereafter. The corresponding dietary protein and lysine intakes required to support maximal protein accretion were 178 g/day (11·7 g/MJ DE) and 13·0 g/day (0·84 g/MJ DE) respectively. Based on the maximal deposition rates for protein (91·8 g/day), and lysine (5·96 g/day) and endogenous protein loss (77middot;6 g/day) estimated from the linear component of the relationship determined between protein deposition and apparent digestible protein intake, the pig's tissue requirements for protein and lysine were only 99·4 g/day (6·5 g/MJ DE) and 6·46 g/day (0·43 g/MJ DE) respectively. This disparity between the pig's tissue protein and amino acid requirements and the dietary levels needed to support these was associated with the fact that the apparent digestibility and biological value of the dietary protein were 0·92 and 0·602 respectively. Apart from small differences in the lysine content of body protein and the methionine: lysine ratio, the average amino acid composition of pigs killed at 8·0 kg, and from the diet of highest protein concentration at 20 kg, was similar to that of ideal protein, indicating that the low utilizability of dietary protein for tissue growth and maintenance was probably associated with low amino acid digestibility and/or availability. The implications of the results with respect to expression of the growing pig's requirements for protein and amino acids are discussed.

Amino acid requirements in inflammatory states

2003 ◽  
Vol 83 (3) ◽  
pp. 365-373 ◽  
Author(s):  
C. Obled
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
De Novo ◽  
Acute Phase Proteins ◽  
Signal Molecules ◽  
Metabolic Disturbances ◽  
Body Protein ◽  
Physiological Processes ◽  
Amino Acid Requirements ◽  
Dispensable Amino Acids

The metabolic disturbances that accompany an inflammatory challenge redirect nutrients from physiological processes important for growth and reproduction toward processes important in host defense. These processes can require increased provision of particular amino acids from the diet in order to spare body protein stores. The pathways that are activated in response to inflammation have to be determined in order to quantify their specific amino acid requirements. For example, increased synthesis of acute phase proteins would require additional supply of specific amino acids according to their amino acid composition. Some dispensable amino acids can become limiting because their de novo synthesis could be impaired and/or be insufficient to cover the increased demands for synthesis of important metabolites. Moreover, amino acids can act on gene expression and as mediators or signal molecules and modulate numerous functions. However, the optimal conditions, especially concentration in physiological liquids, all owing the best expression of these activities are not yet well defined. Key words: Amino acids, requirements, inflammation, protein, metabolism, glutathione, glutamine

Effect of Intraduodenal Starch Infusion on Net Portal Absorption of Amino Acids in Growing steers Fed Lucerne

1994 ◽  
Vol 1994 ◽  
pp. 28-28
Author(s):  
C.J. Seal ◽  
D.S. Parker ◽  
J.C. MacRae ◽  
G.E. Lobley
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Gastrointestinal Tract ◽  
Protein Turnover ◽  
Portal Blood ◽  
Intestinal Lumen ◽  
Short Term ◽  
Net Uptake ◽  
Amino Acid Requirements ◽  
Glucose Availability

Amino acid requirements for energy metabolism and protein turnover within the gastrointestinal tract are substantial and may be met from luminal and arterial pools of amino acids. Several studies have demonstrated that the quantity of amino acids appearing in the portal blood does not balance apparent disappearance from the intestinal lumen and that changing diet or the availability of energy-yielding substrates to the gut tissues may influence the uptake of amino acids into the portal blood (Seal & Reynolds, 1993). For example, increased net absorption of amino acids was observed in animals receiving exogenous intraruminal propionate (Seal & Parker, 1991) and this was accompanied by changes in glucose utilisation by the gut tissues. In contrast, there was no apparent change in net uptake of [l-13C]-leucine into the portal vein of sheep receiving short term intraduodenal infusions of glucose (Piccioli Cappelli et al, 1993). This experiment was designed to further investigate the effects on amino acid absorption of changing glucose availability to the gut with short term (seven hours) or prolonged (three days) exposure to starch infused directly into the duodenum.

Whole-body leucine and lysine metabolism: response to dietary protein intake in young men

1981 ◽  
Vol 240 (6) ◽  
pp. E712-E721 ◽  
Author(s):  
K. J. Motil ◽  
D. E. Matthews ◽  
D. M. Bier ◽  
J. F. Burke ◽  
H. N. Munro ◽  
...  
Keyword(s):  
Amino Acid ◽  
Dietary Protein ◽  
Protein Intake ◽  
Whole Body ◽  
Dietary Protein Intake ◽  
Body Protein ◽  
Fed State ◽  
Amino Acid Requirements ◽  
Maintenance Requirements ◽  
Lysine Metabolism

Whole-body leucine and lysine metabolism was explored in young adult men by a primed constant intravenous infusion of a mixture of L-[1–13C]leucine and L-[alpha-15N]lysine over a 4-h period. Subjects were studied after an overnight fast (postabsorptive state) or while consuming hourly meals (fed state) after adaptation to diets providing either a surfeit level of protein (1.5 g.kg body-1.day-1), a level approximating maintenance requirements (marginal intake) (0.6 g.kg body wt-1.day-1), or a grossly inadequate level (0.1 g.kg-1.day-1). The change in protein intake from a marginal to a surfeit level was associated with an increased leucine flux and incorporation of leucine into body protein. In the fed state, oxidation of leucine increased sharply and release of leucine from tissue protein diminished. When dietary protein intake was reduced from the requirement to inadequate level, leucine flux and body protein synthesis and protein breakdown were reduced, together with a smaller reduction in leucine oxidation. The response of the metabolism of [15N]lysine was responsible for maintenance of leucine and other essential amino acid economy, and they appear to be related to the nitrogen and amino acid requirements of the subject. These findings also demonstrate an effect of meals, modulated by their protein content, on the dynamics of whole-body amino acid metabolism.

scholarly journals Amino acids whose intracellular levels change most during aging alter chronological lifespan of fission yeast

2020 ◽  
Author(s):  
Charalampos Rallis ◽  
Michael Mülleder ◽  
Graeme Smith ◽  
Yan Zi Au ◽  
Markus Ralser ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Fission Yeast ◽  
Yeast Cells ◽  
Total Amino Acid ◽  
Wild Type ◽  
Chronological Lifespan ◽  
Biomarkers Of Aging ◽  
Concentration Changes ◽  
Amino Acid Levels

AbstractAmino acid deprivation or supplementation can affect cellular and organismal lifespan, but we know little about the role of concentration changes in free, intracellular amino acids during aging. Here, we determine free amino-acid levels during chronological aging of non-dividing fission yeast cells. We compare wild-type with long-lived mutant cells that lack the Pka1 protein of the protein kinase A signalling pathway. In wild-type cells, total amino-acid levels decrease during aging, but much less so in pka1 mutants. Two amino acids strongly change as a function of age: glutamine decreases, especially in wild-type cells, while aspartate increases, especially in pka1 mutants. Supplementation of glutamine is sufficient to extend the chronological lifespan of wild-type but not of pka1Δ cells. Supplementation of aspartate, on the other hand, shortens the lifespan of pka1Δ but not of wild-type cells. Our results raise the possibility that certain amino acids are biomarkers of aging, and their concentrations during aging can promote or limit cellular lifespan.

scholarly journals Amino Acid Characteristics of Nigerian Local Cheese (‘Wara’)

2021 ◽  
pp. 1-8
Author(s):  
Adeyeye EI ◽  
◽  
Idowu OT ◽  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Essential Amino Acid ◽  
Crude Protein ◽  
Milk Protein ◽  
Quality Parameters ◽  
Cow Milk ◽  
Amino Acid Requirements ◽  
Excellent Source ◽  
Better Than

This article reports the amino acid composition of the Nigerian local cheese called ‘wara’. ‘Wara’ is made by boiling cow milk with some added coagulant to cuddle the milk protein resulting in coagulated milk protein and whey. ‘Wara’ used to be an excellent source of nutrients such as proteins, fats, minerals and vitamins. Samples were purchased in Ado-Ekiti, Nigeria. Amino acid values were high (g/100g crude protein) in Leu, Asp, Glu, Pro, Phe, Arg with total value of 97.7. The quality parameters of the amino acids were: TEAA (42.6g/100g and 43.6%) whereas TNEAA (55.1g/100g and 56.4%); TArAA (12.8g/100g and 13.1%); TBAA (14.2g/100g and 14.5%); TSAA (3.10g/100g and 3.17%); %Cys in TSAA (51.4); Leu/Ile ratio (1.74); P-PER1 (2.65); P-PER2 (2.48); P-PER3 (2.41); EAAI1 (soybean standard) (1.29) and EAAI2 (egg standard) (99.9); BV (97.2) and Lys/Trp ratio (3.62). The statistical analysis of TEAA/TNEAA at r=0.01 was not significantly different. On the amino acid scores, Met was limiting (0.459) at egg comparison, Lys was limiting at both FAO/WHO [24] and preschool EAA requirements with respective values of 0.966 and 0.97. Estimates of essential amino acid requirements at ages 10-12 years (mg/kg/day) showed the ‘wara’ sample to be better than the standard by 3.72-330% with Lys (3.72%) being least better and Trp (330%) being most. The results showed that ‘wara’ is protein-condensed which can be eaten as raw cheese, flavoured snack, sandwich filling or fried cake.

scholarly journals Multiple Transmembrane Amino Acid Requirements Suggest a Highly Specific Interaction between the Bovine Papillomavirus E5 Oncoprotein and the Platelet-Derived Growth Factor Beta Receptor

2002 ◽  
Vol 76 (16) ◽  
pp. 7976-7986 ◽  
Author(s):  
Valerie M. Nappi ◽  
Lisa M. Petti
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Growth Factor ◽  
Transmembrane Domain ◽  
Specific Interaction ◽  
Platelet Derived Growth Factor ◽  
Helical Conformation ◽  
Bovine Papillomavirus ◽  
E5 Protein ◽  
Amino Acid Requirements

ABSTRACT The bovine papillomavirus E5 protein activates the cellular platelet-derived growth factor β receptor (PDGFβR) tyrosine kinase in a ligand-independent manner. Evidence suggests that the small transmembrane E5 protein homodimerizes and physically interacts with the transmembrane domain of the PDGFβR, thereby inducing constitutive dimerization and activation of this receptor. Amino acids in the receptor previously found to be required for the PDGFβR-E5 interaction are a transmembrane Thr513 and a juxtamembrane Lys499. Here, we sought to determine if these are the only two receptor amino acids required for an interaction with the E5 protein. Substitution of large portions of the PDGFβR transmembrane domain indicated that additional amino acids in both the amino and carboxyl halves of the receptor transmembrane domain are required for a productive interaction with the E5 protein. Indeed, individual amino acid substitutions in the receptor transmembrane domain identified roles for the extracellular proximal transmembrane residues in the interaction. These data suggest that multiple amino acids within the transmembrane domain of the PDGFβR are required for a stable interaction with the E5 protein. These may be involved in direct protein-protein contacts or may support the proper transmembrane alpha-helical conformation for optimal positioning of the primary amino acid requirements.

Free Amino Acid and Haemolymph Concentration Changes in Sphaeroma Rugicauda (Isopoda) During Adaptation to a Dilute Salinity

1969 ◽  
Vol 50 (2) ◽  
pp. 319-326
Author(s):  
R. R. HARRIS
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Free Amino Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Sea Water ◽  
Protein Nitrogen ◽  
Body Sodium ◽  
Concentration Changes ◽  
Total Body

1. Non-protein and protein nitrogen fractions of the isopod Sphaeroma rugicauda were measured in animals adapted to 100 and 2% sea water. 2. The non-protein nitrogen component was reduced in animals acclimatized to the lower salinity. 3. Free amino acids accounted for 88 and 74% respectively of the non-protein nitrogen in the two salinities. 4. In 2% sea water taurine, proline, glycine, alanine and glutamic acid showed the greatest decreases in concentration compared to the levels measured in animals adapted to 100% sea water. 5. The decrease in total free amino acids of animals acclimatized to 100% sea water and transferred to 2% sea water was measured. 6. The total free amino acid concentration is reduced to the 2% sea water level within 12 hr. after transfer. 7. Free amino acid, haemolymph sodium and total body sodium levels after transfer to 2% sea water were compared. 8. The asymmetry between the fall in haemolymph sodium concentration and the decrease in total body sodium under these conditions is thought to be due to a water shift from the haemolymph into the tissues. 9. It is suggested that the osmotic pressure of the cells falls at a slower rate than that of the haemolymph.

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