Protein nitrogen, peptide nitrogen and free amino acid nitrogen in endogenous digesta nitrogen at the terminal ileum of the rat

1992 ◽  
Vol 59 (3) ◽  
pp. 291-298 ◽  
Author(s):  
Christine A Butts ◽  
Paul J Moughan ◽  
William C Smith
Keyword(s):  
Amino Acid ◽  
Free Amino Acid ◽  
Terminal Ileum ◽  
Free Amino ◽  
Protein Nitrogen ◽  
Amino Acid Nitrogen

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.

Use of a Peptide Rather Than Free Amino Acid Nitrogen Source in Chemically Defined “Elemental” Diets

1980 ◽  
Vol 4 (6) ◽  
pp. 548-553 ◽  
Author(s):  
David B. A. Silk ◽  
Peter D. Fairclough ◽  
Michael L. Clark ◽  
John E. Hegarty ◽  
Jill M. Addison ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nitrogen Source ◽  
Free Amino Acid ◽  
Free Amino ◽  
Amino Acid Nitrogen ◽  
Elemental Diets

Effects of glucocorticoids on glutamine metabolism in skeletal muscle

1984 ◽  
Vol 247 (1) ◽  
pp. E75-E83 ◽  
Author(s):  
F. Muhlbacher ◽  
C. R. Kapadia ◽  
M. F. Colpoys ◽  
R. J. Smith ◽  
D. W. Wilmore
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Free Amino Acid ◽  
Free Amino ◽  
Glutamine Metabolism ◽  
Glutamine Concentration ◽  
Amino Acid Nitrogen ◽  
Flux Measurements ◽  
Altered Metabolism

The effects of dexamethasone on nitrogen and amino acid metabolism in the dog were studied in order to gain insight into the role of glucocorticoids in accelerated proteolysis and altered metabolism of glutamine in catabolic illnesses. After dexamethasone administration at a dose of 0.44 mg X day-1 X kg-1, nitrogen balance shifted from slightly positive (+0.126 g N X day-1 X kg-1) to markedly negative (-0.278 g N X day-1 X kg-1). This was associated with a 23% fall in total free amino acid nitrogen in skeletal muscle, with 80% of the decline accounted for by a decrease in glutamine. Plasma glutamine concentration decreased by 26%, although total plasma free amino acid nitrogen was unchanged because of a 49% increase in alanine. The alterations in intracellular and circulating levels of glutamine were not accompanied by measurable changes in glutamine synthetase or glutaminase activities in skeletal muscle. Hindquarter amino acid flux measurements demonstrated that the decline in intracellular glutamine concentration was associated with a marked increase in glutamine efflux from skeletal muscle. This occurred in spite of minimal changes in the intracellular/extracellular glutamine gradient. It is concluded that accelerated muscle glutamine release caused by glucocorticoids is a major contributor to the decreased glutamine levels in muscle that occur during critical illnesses.

Effects of Nitrogen Source and Concentration on the Free Amino Acid Composition of Developing Wheat Grains

1990 ◽  
Vol 17 (2) ◽  
pp. 199 ◽  
Author(s):  
C Blumenthal ◽  
JW Lee ◽  
EWR Barlow ◽  
IL Batey
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Ammonium Nitrate ◽  
Amino Acid Composition ◽  
Free Amino Acid ◽  
Acid Composition ◽  
Free Amino ◽  
Amino Nitrogen ◽  
Grain Protein ◽  
Protein Nitrogen

Detached wheat heads (7 days post-anthesis) were grown in liquid culture containing nitrogen concentrations of 0.025% or 0.1% in the form of glutamine, ammonium nitrate or asparagine. With each form of the nitrogen, increasing the concentrations of nitrogen in the culture medium led to increases in the total nitrogen and the non-protein nitrogen in the grain. Protein contents (N × 5.7) were approximately 16% and 21% on a dry weight basis in the low and high treatments respectively for all nitrogen sources. Amino acids from the endosperm cavity, the ethanol-soluble extract of the grain, and the grain protein were analysed by HPLC techniques to define the site of transfer between amino acid forms. The results indicated that amino nitrogen from glutamine, ammonium nitrate, or asparagine enters the grain and is found in the endosperm cavity fluid mainly in the form of glutamine, alanine and, to a lesser extent, aspartate (including asparagine). These amino acids are then converted into the various other amino acids required for protein synthesis, as is demonstrated by the increases found in the others in the ethanol-soluble free amino acid fraction with different nitrogen regimes. These variations in the composition of the free amino acids occurred without altering the amino acid composition of the protein component of the grain.

Effect of breed on proteolysis and free amino acid profiles of dry-cured loin during processing

2019 ◽  
Vol 59 (6) ◽  
pp. 1161 ◽  
Author(s):  
Eva Salazar ◽  
José M. Cayuela ◽  
Adela Abellán ◽  
Luis Tejada
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Free Amino Acid ◽  
Proteolytic Activity ◽  
Free Amino Acids ◽  
Free Amino ◽  
Processing Time ◽  
Point Of View ◽  
Protein Nitrogen ◽  
Amino Acid Profiles

Non-protein nitrogen (NPN) and free amino acids (FAA) were analysed in dry-cured loin obtained from the native pig breed Chato Murciano (CM) during processing. In addition, a comparison was drawn between the NPN and FAA values obtained in CM and those obtained in dry-cured loin from a modern crossbreed pig genotype (CG) at commercialisation times (between 30 and 60 days of processing). Processing time affected NPN, total FAA concentration, and all FAA studied, except arginine, histidine and lysine. The breed affected both NPN and total FAA, as superior values were observed in CM at Day 30. From this moment onward, proteolysis was more intense in CG than in CM. At Day 30, the concentration of most amino acids, except for lysine and arginine, was higher in CM. Whereas the concentration of all amino acids, except serine, histidine and methionine + tryptophan, was higher in CG at Day 60. The breed affected proteolytic activity in dry-cured loin. The results suggested that, from the point of view of proteolysis, the optimum processing time for CM dry-cured loin is 45 days.

scholarly journals ALTERATION IN CARBOHYDRATE METABOLISM BY SUB-ACUTE LEAD EXPOSURE: A DOSE-DEPENDENT STUDY

2017 ◽  
Vol 9 (3) ◽  
pp. 254
Author(s):  
Pritha Das ◽  
Sudipta Pal
Keyword(s):  
Body Weight ◽  
Amino Acid ◽  
Free Amino Acid ◽  
Pyruvic Acid ◽  
Pyruvate Dehydrogenase ◽  
Enzyme Activities ◽  
Free Amino ◽  
Weight Group ◽  
Amino Acid Nitrogen ◽  
Dose Dependent

Objective: The study was conducted to evaluate the dose-dependent effects of sub-acute lead exposure on certain aspects of carbohydrate metabolism.Methods: Swiss albino male mice (weighing 30-35 g) were selected for the present study and divided into five groups; one control group and others lead-treated groups i.e. Group A (5 mg/kg body weight), Group B (10 mg/kg body weight), Group C (15 mg/kg body weight) and Group D (20 mg/kg body weight). Parameters like blood and liver glucose, glycogen and pyruvic acid contents were determined in liver tissue. The enzyme activities like pyruvate dehydrogenase, malate dehydrogenase and glucose 6-phosphatase were recorded in that tissue. Additionally, free amino acid nitrogen content and transaminase enzyme activities were also evaluated in liver tissue of mice.Results: The study reveals that lead caused a significant diminution of blood and hepatic glucose levels and fall in liver glycogen content in a dose-dependent manner, the highest effect was observed in animals treated with lead at a dose of 20 mg/kg body weight. Glucose 6-phosphatase activity was decreased significantly in all the treated groups. There was a dose-dependent increase in pyruvic acid content whereas pyruvate dehydrogenase, malate dehydrogenase and transaminase enzyme activities were significantly depressed in a dose-dependent fashion in all the treated animals. Additionally, lead treatment significantly (p<0.001) enhanced free amino acid nitrogen in the liver to provide a substrate for gluconeogenesis.Conclusion: It is suggested that an adaptive mechanism is initiated by stimulating and retarding glycogenolytic and glycolytic activity and also by rising in the content of free amino acid nitrogen to recover from the lead stressed toxic manifestation

Amino acid pool composition of the basidiomyceteCoprinus cinereus

2007 ◽  
Vol 53 (11) ◽  
pp. 1278-1281 ◽  
Author(s):  
Cynthia E. Ulrich ◽  
Allen C. Gathman ◽  
Walt W. Lilly
Keyword(s):  
Amino Acid ◽  
Nitrogen Source ◽  
Free Amino Acid ◽  
Free Amino ◽  
Nitrogen Availability ◽  
Amino Acid Pool ◽  
Nitrogen Deprivation ◽  
High Concentration ◽  
Protein Nitrogen ◽  
Acid Pool

The leaf-litter fungus Coprinus cinereus maintains a pool of free amino acid in its mycelium. When the organism is grown under conditions of high nitrogen availability with 13.2 mmol·L–1l-asparagine as the nitrogen source, the primary constituents of this pool are glutamine, alanine, and glutamic acid. Together these 3 amino acids comprise approximately 70% of the pool. Nitrogen deprivation reduces the size of the free amino acid pool by 75%, and neither a high concentration of ammonium nor a protein nitrogen source support a similar pool size as l-asparagine. Nitrogen deprivation also reduces the concentration of glutamine to the pool while increasing glutamate. Concomitant with this shift is a marked increase in mycelial ammonium.

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