scholarly journals HEMOGLOBIN AND PLASMA PROTEIN

1943 ◽  
Vol 77 (4) ◽  
pp. 375-396 ◽  
Author(s):  
F. S. Robscheit-Robbins ◽  
L. L. Miller ◽  
G. H. Whipple
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Plasma Protein ◽  
The Body ◽  
Acid Mixture ◽  
Blood Proteins ◽  
Body Protein ◽  
Growth Mixture ◽  
Amino Acid Mixtures ◽  
Hemoglobin Production

Given healthy dogs, fed abundant iron and protein-free or low protein diets, with sustained anemia due to bleeding, we can study the capacity of these animals to produce simultaneously new hemoglobin and plasma protein. The reserve stores of blood protein producing materials in this way are very largely depleted, and levels of 6 to 8 gm. per cent for hemoglobin and 4 to 5 gm. per cent for plasma protein can be maintained for considerable periods of time. These dogs are very susceptible to infection and to injury by many poisons. Under such conditions, these anemic and hypoproteinemic dogs will use very efficiently a variety of digests (serum, hemoglobin, and casein) and the growth mixture (Rose) of pure amino acids. Nitrogen balance is maintained and considerable new blood proteins are produced. Dog plasma by vein is used freely in these doubly depleted dogs to make new hemoglobin in abundance (Table 1). Serum digests by vein are well utilized to make new hemoglobin and plasma protein in the same dogs (Table 1). Serum digests by mouth are effectively used to make new blood proteins (Table 5). Dog or sheep hemoglobin given in large amounts intraperitoneally are remarkably well utilized to form hemoglobin and plasma protein (Table 6). It must be obvious that the globin of the hemoglobin is saved in these protein-depleted dogs and used to make large amounts of hemoglobin and plasma protein. Hemoglobin digests are also well utilized whether given by mouth (Table 7) or by vein (Table 8) and liberal amounts of plasma protein are manufactured from digests presumably ideally suited for hemoglobin production. Casein digests are well used (Table 8) and form as much new plasma protein as any material tested—even serum digests. Amino acid mixtures are of especial interest. The growth mixture of 10 amino acids (Rose) is well utilized by mouth or by vein and favors new hemoglobin production more than any material tested (Table 2). Cystine replacing methionine in the amino acid mixture increases the plasma protein—hemoglobin output ratio, that is it favors plasma protein production. Digests of various sorts and amino acid mixtures or combinations of digests and amino acid mixtures can be used rapidly and effectively to build new hemoglobin or plasma protein, to maintain nitrogen equilibrium, and to replete reserve protein stores. These experiments point to clinical problems. The unexplained preference given to hemoglobin production in these hypoproteinemic dogs is observed under all conditions, even when whole plasma or serum digests are given by vein. In general, 2 to 4 gm. of hemoglobin are formed for every gram of plasma protein. This all adds up to a remarkable fluidity in the use of plasma protein or hemoglobin which can contribute directly to the body protein pool from which are evolved, without waste of nitrogen, the needed proteins, whether hemoglobin, plasma protein, or tissue proteins.

scholarly journals TEN AMINO ACIDS ESSENTIAL FOR PLASMA PROTEIN PRODUCTION EFFECTIVE ORALLY OR INTRAVENOUSLY

1943 ◽  
Vol 77 (3) ◽  
pp. 277-295 ◽  
Author(s):  
S. C. Madden ◽  
J. R. Carter ◽  
A. A. Kattus ◽  
L. L. Miller ◽  
G. H. Whipple
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Plasma Protein ◽  
Nitrogen Balance ◽  
Protein Intake ◽  
Protein Production ◽  
The Body ◽  
Acid Mixture ◽  
Negative Nitrogen Balance ◽  
Growth Mixture

When blood plasma proteins are depleted by bleeding with return of the washed red cells (plasmapheresis) it is possible to bring dogs to a steady state of hypoproteinemia and a constant level of plasma protein production if the diet protein intake is controlled and limited. Such dogs are outwardly normal but have a lowered resistance to infection and to certain intoxications. When the protein intake of such dogs is completely replaced by the growth mixture (Rose) of crystalline amino acids, plasma protein production is excellent, weight and nitrogen balance are maintained. This growth mixture consists of ten amino acids, threonine, valine, leucine, isoleucine, tryptophane, lysine, phenylalanine, methionine, histidine, arginine, and is as effective as most diet proteins in plasma protein production. The above amino acid mixture in aqueous solution may be given by vein with equally good plasma protein production and no apparent clinical disturbance even when given rapidly. Cystine may replace methionine in the above mixture with equally good plasma protein production for 7 to 10 days but at the expense of the body tissues, that is, with weight loss and a negative nitrogen balance. The addition of cystine to the protein-free, otherwise adequate diet may result in the production of considerable new plasma protein during a period as long as 1 week (cystine effect). This reaction may depend upon the amino acid constitution of the preceding diet protein in that it occurred following a liver feeding but did not occur after pancreas feeding. Arginine is required in the diet of the protein depleted dog for fabrication of plasma protein. It is apparently not needed for nitrogen balance for as long as 1 or 2 weeks. The omission of either threonine or valine from the growth mixture is quickly followed by a sharp decline in plasma protein formation and by a negative nitrogen balance. When histidine, arginine, and most of the lysine are omitted from the growth mixture, nitrogen balance and weight may be maintained for as long as 1 week but plasma protein production falls off markedly. The findings indicate that the growth mixture of amino acids should be a valuable addition to transfusion and infusion therapy in disease states associated with deficient nitrogen intake or tissue injury and accelerated nitrogen loss, including shock, burns, and major operative procedures.

scholarly journals PLASMA PROTEIN AND HEMOGLOBIN PRODUCTION

1947 ◽  
Vol 85 (3) ◽  
pp. 243-265 ◽  
Author(s):  
F. S. Robscheit-Robbins ◽  
L. L. Miller ◽  
G. H. Whipple
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Plasma Protein ◽  
Nitrogen Balance ◽  
Essential Amino Acids ◽  
Amino Acid Mixture ◽  
Blood Protein ◽  
Acid Mixture ◽  
Amino Acid Mixtures ◽  
Urinary Nitrogen

Given healthy dogs fed abundant iron and protein-free or low protein diets with sustained anemia and hypoproteinemia, we can study the capacity of these animals to produce simultaneously new hemoglobin and plasma protein. Reserve stores of blood protein-building materials are measurably depleted and levels of 6 to 8 gm. per cent for hemoglobin and 4 to 5 gm. per cent for plasma protein can be maintained for weeks or months depending upon the intake of food proteins or amino acid mixtures. These dogs are very susceptible to infection and various poisons. Dogs tire of these diets and loss of appetite terminates many experiments. Under these conditions (double depletion) standard growth mixtures of essential amino acids are tested to show the response in blood protein output and urinary nitrogen balance. As a part of each tabulated experiment one of the essential amino acids is deleted from the complete growth mixture to compare such response with that of the whole mixture. Methionine, threonine, phenylalanine, and tryptophane when singly eliminated from the complete amino acid mixture do effect a sharp rise in urinary nitrogen. This loss of urinary nitrogen is corrected when the individual amino acid is replaced in the mixture. Histidine, lysine, and valine have a moderate influence upon urinary nitrogen balance toward nitrogen conservation. Leucine, isoleucine, and arginine have minimal or no effect upon urinary nitrogen balance when these individual amino acids are deleted from the complete growth mixture of amino acids during 3 to 4 week periods. Tryptophane and to a less extent phenylalanine and threonine when returned to the amino acid mixture are associated with a conspicuous preponderance of plasma protein output over the hemoglobin output (Table 4). Arginine, lysine, and histidine when returned to the amino acid mixture are associated with a large preponderance of hemoglobin output. Various amino acid mixtures under these conditions may give a positive urinary nitrogen balance and a liberal output of blood proteins but there is always weight loss, however we may choose to explain this loss. These experiments touch on the complex problems of parenteral nutrition, experimental and clinical.

scholarly journals Effect of co-ingestion of amino acids with rice on glycaemic and insulinaemic response

2015 ◽  
Vol 114 (11) ◽  
pp. 1845-1851 ◽  
Author(s):  
Yean Yean Soong ◽  
Joseph Lim ◽  
Lijuan Sun ◽  
Christiani Jeyakumar Henry
Keyword(s):  
Amino Acids ◽  
Blood Glucose ◽  
Amino Acid ◽  
Glycaemic Index ◽  
Amino Acid Mixture ◽  
Postprandial Blood Glucose ◽  
Acid Mixture ◽  
White Rice ◽  
Amino Acid Mixtures

AbstractConsumption of high glycaemic index (GI) and glycaemic response (GR) food such as white rice has been implicated in the development of type 2 diabetes. Previous studies have reported the ability of individual amino acids to reduce GR of carbohydrate-rich foods. Because of the bitter flavour of amino acids, they have rarely been used to reduce GR. We now report the use of a palatable, preformed amino acid mixture in the form of essence of chicken. In all, sixteen healthy male Chinese were served 68 or 136 ml amino acid mixture together with rice, or 15 or 30 min before consumption of white rice. Postprandial blood glucose and plasma insulin concentrations were measured at fasting and every 15 min after consumption of the meal until 60 min after the consumption of the white rice. Subsequent blood samples were taken at 30-min intervals until 210 min. The co-ingestion of 68 ml of amino acid mixture with white rice produced the best results in reducing the peak blood glucose and GR of white rice without increasing the insulinaemic response. It is postulated that amino acid mixtures prime β-cell insulin secretion and peripheral tissue uptake of glucose. The use of ready-to-drink amino acid mixtures may be a useful strategy for lowering the high-GI rice diets consumed in Asia.

Consistency and Change

2019 ◽  
Author(s):  
Alan Kelly
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Living Organism ◽  
Peptide Bond ◽  
The Body ◽  
Blood Proteins ◽  
Genes Encoding ◽  
Fundamental Phenomenon ◽  
P Proteins

Proteins are, in my view, the most impressive molecules in food. They influence the texture, crunch, chew, flow, color, flavor, and nutritional quality of food. Not only that, but they can radically change their properties and how they behave depending on the environment and, critically for food, in response to processes like heating. Even when broken down into smaller components they are important, for example giving cheese many of its critical flavor notes. Indeed, I would argue that perhaps the most fundamental phenomenon we encounter in cooking or processing food is the denaturation of proteins, as will be explained shortly. Beyond food, the value of proteins and their properties is widespread across biology. Many of the most significant molecules in our body and that of any living organism (including plants and animals) are proteins. These include those that make hair and skin what they are, as well as the hemoglobin that transports oxygen around the body in our blood. Proteins are built from amino acids, a family of 20 closely related small molecules, which all have in chemical terms the same two ends (chemically speaking, an amino end and an acidic end, hence the name) but differ in the middle. This bit in the middle varies from amino acid to amino acid, from simple (a hydrogen atom in the case of glycine, the simplest amino acid) to much more complex structures. Amino acids can link up very neatly, as the amino end of one can form a bond (called a peptide bond) with the acid end of another, and so forth, so that chains of amino acids are formed that, when big enough (more than a few dozen amino acids), we call proteins. Our bodies produce thousands of proteins for different functions, and the instructions for which amino acids combine to make which proteins are essentially what the genetic code encrypted in our DNA specifies. We hear a lot about our genes encoding the secrets of life, but what that code spells is basically P-R-O-T-E-I-N. Yes, these are very important molecules!

scholarly journals Conversion Percentage of Tryptophan to Nicotinamide is Higher in Rice Protein Diet than in Wheat Protein Diet in Rats

2015 ◽  
Vol 8 ◽  
pp. IJTR.S22444
Author(s):  
Katsumi Shibata ◽  
Tsutomu Fukuwatari ◽  
Tomoyo Kawamura
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Body Weight Gain ◽  
Acid Value ◽  
Amino Acid Mixture ◽  
The Body ◽  
Protein Diet ◽  
Acid Mixture ◽  
Wheat Protein ◽  
Rice Protein

We reported previously that the pellagragenic property of corn protein is not only low L-tryptophan concentration but also the lower conversion percentage of L-tryptophan to nicotinamide; the amino acid composition greatly affected the conversion percentage. The amino acid value of wheat protein is lower than that of rice protein. In the present study, we compare the conversion percentages of L-tryptophan to nicotinamide between wheat protein and rice protein diets in growing rats. The body weight gain for 28 days in rats fed with a 10% amino acid mixture diet with wheat protein was lower than that of rats fed with a 10% amino acid diet with rice protein (68.1 ± 1.6 g vs 108.4 ± 1.9 g; P < 0.05). The conversion percentage of L-tryptophan to nicotinamide was also lower for the wheat protein diet compared with the rice protein diet (1.44 ± 0.036% vs 2.84 ± 0.19%; P < 0.05). The addition of limiting amino acids (L-isoleucine, L-lysine, L-tryptophan, L-methionine, L-threonine) to the wheat protein diet improved growth and the conversion percentage. In conclusion, our result supports the thinking that the composition of amino acids affects the conversion ratio of L-tryptophan to nicotinamide.

scholarly journals Splanchnic-bed transfers of amino acids in sheep blood and plasma, as monitored through use of a multiple U-13C-labelled amino acid mixture

1996 ◽  
Vol 75 (2) ◽  
pp. 217-235 ◽  
Author(s):  
G. E. Lobley ◽  
A. Connell ◽  
D. K. Revell ◽  
B. J. Bequette ◽  
D. S. Brown ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Essential Amino Acids ◽  
Whole Body ◽  
Gas Chromatography Mass Spectrometry ◽  
Acid Mixture ◽  
Body Protein ◽  
Hydrolysis Of

AbstractThe response in whole-body and splanchnic tissue mass and isotope amino acid transfers in both plasma and blood has been studied in sheep offered 800 g lucerne (Medicago sutiva) pellets/d. Amino acid mass transfers were quantified over a 4 h period,by arterio-venous procedures, across the portal-drained viscera (PDV) and liver on day 5 of an intravenous infusion of either vehicle or the methylated products, choline (0.5 g/d) plus creatine (10 g/d). Isotopic movements were monitored over the same period during a 10 h infusion of a mixture of U-13C-labelled amino acids obtained from hydrolysis of labelled algal cells. Sixteen amino acids were monitored by gas chromatography-mass spectrometry, with thirteen of these analysed within a single chromatographic analysis. Except for methionine, which is discussed in a previous paper, no significant effects of choline plus creatine infusion were observed on any of the variables reported. Whole-body protein irreversible-loss rates ranged from 158 to 245 g/d for the essential amino acids, based on the relative enrichments (dilution of the U-13C molecules by those unlabelled) of free amino acids in arterial plasma, and 206-519 g/d, when blood free amino acid relative enrichments were used for the calculations. Closer agreement was obtained between lysine, threonine, phenylalanine and the branched-chain amino acids. Plasma relative enrichments always exceeded those in blood (P < 0.001), possibly due to hydrolysis of peptides or degradation of protein within the erythrocyte or slow equilibration between plasma and the erythrocyte. Net absorbed amino acids across the PDV were carried predominantly in the plasma. Little evidence was obtained of any major and general involvement of the erythrocytes in the transport of free amino acids from the liver. Net isotope movements also supported these findings. Estimates of protein synthesis rates across the PDV tissues from [U-13C] leucine kinetics showed good agreement with previous values obtained with single-labelled leucine. Variable rates were obtained between the essential amino acids, probably due to different intracellular dilutions. Isotope dilution across the liver was small and could be attributed predominantly to uni-directional transfer from extracellular sources into the hepatocytes and this probably dominates the turnover of the intracellular hepatic amino acid pools.

scholarly journals PLASMA PROTEIN PRODUCTION INFLUENCED BY AMINO ACID MIXTURES AND LACK OF ESSENTIAL AMINO ACIDS

1945 ◽  
Vol 82 (2) ◽  
pp. 77-92 ◽  
Author(s):  
S. C. Madden ◽  
F. W. Anderson ◽  
J. C. Donovan ◽  
G. H. Whipple
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Plasma Protein ◽  
Protein Production ◽  
Daily Intake ◽  
Essential Amino Acids ◽  
Nitrogen Excretion ◽  
Acid Mixture ◽  
Rapid Weight Loss ◽  
Urinary Nitrogen

When blood plasma proteins are depleted by bleeding with return of red cells suspended in saline (plasmapheresis) it is possible to bring dogs to a steady state of hypoproteinemia and a constant level of plasma protein production if the diet nitrogen intake is controlled and limited. Such dogs are outwardly normal but have a lowered resistance to infection and intoxication and probably to vitamin deficiency. When the diet nitrogen is provided by certain mixtures of the ten growth essential amino acids plus glycine, given intravenously at a rapid rate, plasma protein production is good. The same mixture absorbed subcutaneously at a slower rate may be slightly better utilized. Fed orally the same mixture is better utilized and associated with a lower urinary nitrogen excretion. An ample amino acid mixture for the daily intake of a 10 kilo dog may contain in grams dl-threonine 1.4, dl-valine 3, dl-leucine 3, dl-isoleucine 2, l(+)-lysine·HCl·H2O 2.2, dl-tryptophane 0.3, dl-phenylalanine 2, dl-methionine 1.2, l(+)-histidine·HCl·H2O 1, l(+)-arginine·HCl 1, and glycine 2. Half this quantity is inadequate and not improved by addition of a mixture of alanine, serine, norleucine, proline, hydroxyproline, and tyrosine totalling 1.4 gm. Aspartic acid appears to induce vomiting when added to a mixture of amino acids. The same response has been reported for glutamic acid (8). Omission from the intake of leucine or of leucine and isoleucine results in negative nitrogen balance and rapid weight loss but plasma protein production may be temporarily maintained. It is possible that leucine may be captured from red blood cell destruction. Tryptophane deficiency causes an abrupt decline in plasma protein production. No decline occurred during 2 weeks of histidine deficiency but the urinary nitrogen increased to negative balance. Plasma protein production may be impaired during conditions of dietary deficiency not related to the protein or amino acid intake. Skin lesions and liver function impairment are described. Unidentified factors present in liver and yeast appear to be involved.

scholarly journals Allometric growth of protein, amino acids, fat and minerals in slow- and fast-growing young chickens

2011 ◽  
Vol 56 (No. 3) ◽  
pp. 127-135 ◽  
Author(s):  
J. Zelenka ◽  
J. Heger ◽  
S. Kráčmar ◽  
E. Mrkvicová
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nitrogen Retention ◽  
Growth Period ◽  
The Body ◽  
Allometric Growth ◽  
Retention Efficiency ◽  
Body Protein ◽  
Fast Growing ◽  
Protein Amino Acids

Allometric growth of body constituents and apparent efficiency of amino acid and nitrogen retention were examined in slow-growing laying-type cockerels (SG) and in fast-growing male broiler hybrids (FG) during the growth period from hatch to Day 22. The respective allometric coefficients for water, protein, (N &times; 6.25)ash and fat in relation to body weight were 0.971, 1.080, 1.096 and 1.284 for SG chickens and 0.977, 1.099, 0.993, and 1.198 for FG chickens. The respective allometric coefficients describing the relationships of water, fat and ash weight with protein weight were 0.894, 1.014, and 1.186 for SG chickens and 0.893, 0.910, and 1.097 for FG chickens. High allometric coefficients for ash in both genotypes likely indicate the rapid growth of skeletal tissues which requires adequate mineral nutrition during this period of growth. The deposition of ash relative to protein was significantly higher (P &lt; 0.05) in SG chickens thus suggesting that the relative growth of ash may be affected by genotype. Allometric coefficients relating amino acids to body protein were less than unity in most cases which indicates that an increasing amount of non-protein N is deposited in the body with advancing age. Except for cysteine, the apparent efficiency of amino acid retention was lower in SG as compared to FG chickens. The high retention efficiency of cysteine in SG genotype was likely associated with the conversion of surplus methionine to cysteine, required for feather protein synthesis in laying-type birds at an early age.

scholarly journals Jejunal absorption of an amino acid mixture simulating casein and an enzymic hydrolysate of casein prepared for oral administration to normal adults

1975 ◽  
Vol 33 (1) ◽  
pp. 95-100 ◽  
Author(s):  
D. B. A. Silk ◽  
M. L. Clark ◽  
T. C. Marrs ◽  
Jill M. Addison ◽  
D. Burston ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Oral Administration ◽  
Human Subjects ◽  
Amino Nitrogen ◽  
Casein Hydrolysate ◽  
Amino Acid Mixture ◽  
Acid Mixture ◽  
Amino Acid Mixtures ◽  
Percentage Absorption

1. An intestinal perfusion technique was used in six normal human subjects to study absorption of sixteen individual amino acids from an amino acid mixture simulating casein and from an enzymic hydrolysate of casein, prepared for oral administration to these subjects, which consisted of a mixture of oligopeptides and free amino acids.2. Total absorption of α-amino nitrogen was greater from the casein hydrolysate than from the amino acid mixture, and the considerable variation in percentage absorption of individual amino acids from the amino acid mixture was much reduced when the enzymic hydrolysate solution was perfused, as a number of amino acids which were poorly absorbed from the amino acid mixture were absorbed to a greater extent from the casein hydrolysate.3. These findings indicate that after extensive intestinal resections or in malabsorption there might be significant nutritional advantages in the administration of protein hydrolysates rather than amino acid mixtures.

Amino Acid Concentrations in Portal Venous Plasma during Absorption from the Small Intestine of the Guinea Pig of an Amino Acid Mixture Simulating Casein and a Partial Enzymic Hydrolysate of Casein

1977 ◽  
Vol 52 (3) ◽  
pp. 259-267
Author(s):  
M. H. Sleisenger ◽  
D. Pelling ◽  
D. Burston ◽  
D. M. Matthews
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Guinea Pig ◽  
Preliminary Investigation ◽  
Amino Acid Mixture ◽  
Acid Mixture ◽  
Analytical Technique ◽  
Amino Acid Mixtures ◽  
Amino Acid Concentrations ◽  
Venous Plasma

1. The characteristics of absorption of individual amino acids from amino acid mixtures simulating casein and from enzymic hydrolysates of casein containing oligopeptides as well as free amino acids are known to be different. The differences, which are attributable to mucosal uptake of small peptides, involve more rapid absorption from the enzymic hydrolysates of certain amino acids which are relatively slowly absorbed from the amino acid mixtures. This could lead to more effective utilization of amino acids from the enzymic hydrolysates than from the amino acid mixtures. 2. To obtain further information bearing on this hypothesis, we have used a recently developed technique for portal cannulation in the guinea pig to make a preliminary investigation of amino acid concentrations in the portal venous plasma at intervals after the infusion into the duodenum of equivalent amounts of (a) an amino acid mixture simulating casein and (b) a partial enzymic (papain followed by kidney peptidases) hydrolysate of casein, the two preparations being infused in separate experiments. 3. For some amino acids, such as leucine, isoleucine, valine, phenylalanine and lysine, the curves after the enzymic hydrolysate were fairly similar to the corresponding curves after the amino acid mixture, though usually slightly lower. With other amino acids, the curves after the enzymic hydrolysate were very much lower than the corresponding curves after the amino acid mixture. With serine, glutamine, proline and glycine this discrepancy was particularly great. 4. The results cannot yet be fully explained, but their main features are explicable by the hypothesis that the lower amino acid concentrations in portal plasma after the enzymic hydrolysate are the result of entry of amino acids into the portal blood in peptide form, in which they would not be detectable by the analytical technique employed, and possibly also of more rapid clearance of amino acids from the blood during absorption of this preparation.

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