scholarly journals THE INFLUENCE OF NITROGEN RETENTION UPON THE REGENERATION OF PLASMA PROTEINS

1940 ◽  
Vol 71 (3) ◽  
pp. 299-304 ◽  
Author(s):  
Russell L. Holman ◽  
J. Gilmer Mebane
Keyword(s):  
Blood Plasma ◽  
Plasma Protein ◽  
Renal Injury ◽  
Plasma Proteins ◽  
Protein Production ◽  
Clinical Observation ◽  
Nitrogen Retention ◽  
Blood Plasma Protein ◽  
Uranium Nitrate ◽  
Per Se

1. Because of the clinical observation that the capacity to form new plasma proteins is sometimes impaired in cases of nephritis (2), experiments were performed to determine whether the impaired function in the nephritic is related to nitrogen retention. 2. These experiments consisted of producing renal injury by injecting uranium nitrate into standard hypoproteinemic dogs and comparing the rate of blood plasma protein formation under these conditions of nitrogen retention with that in the uninjured dog. 3. Despite elevations in blood N.P.N. to more than ten times normal, no interference with plasma protein formation was observed. These elevations in N.P.N. affected principally the urea and undetermined fractions. 4. Neither elevation in N.P.N. nor proteinuria per se appears to have any effect upon plasma protein production. Possibly the deficient production of plasma proteins in the nephritic is related to a more general disturbance in metabolism in which the elevation in N.P.N. is secondary.

scholarly journals BLOOD PLASMA PROTEIN REGENERATION AS INFLUENCED BY INFECTION, DIGESTIVE DISTURBANCES, THYROID, AND FOOD PROTEINS

1937 ◽  
Vol 65 (3) ◽  
pp. 431-454 ◽  
Author(s):  
S. C. Madden ◽  
P. M. Winslow ◽  
J. W. Rowland ◽  
G. H. Whipple
Keyword(s):  
Blood Plasma ◽  
Plasma Protein ◽  
Plasma Proteins ◽  
Protein Production ◽  
Building Materials ◽  
Basal Diet ◽  
The Body ◽  
Potency Ratio ◽  
Blood Plasma Protein ◽  
Diet Intake

When blood plasma proteins are depleted by bleeding, with return of washed red cells (plasmapheresis), it is possible to bring dogs to a steady state of low plasma protein in the circulation and a uniform plasma protein production on a basal diet. Such dogs become test subjects by which the effect of various factors on plasma protein regeneration can be measured. Dogs previously the subjects of plasmapheresis, during long rest periods appear to increase their stores of plasma protein building materials and their blood plasma protein concentrations above former normal levels. A sterile abscess (turpentine) induces a marked reduction in plasma protein regeneration in these test dogs consuming an ample basal diet. The sharp reduction during the initial 24 hours may in part reflect an extravasation of plasma protein into the injured tissue but there also appears to develop a true disturbance of the mechanism which produces plasma proteins. Digestive disturbances interfere seriously with plasma protein production. Whereas large quantities of live yeast upset digestion and form no plasma protein, autoclaved yeast is well utilized, having a potency ratio of 4.4. Amino acids have been tested inadequately. A mixture of cystine, glutamic acid, and glycine does seem to have a definite effect upon protein metabolism and plasma protein production. Iron, under the conditions of these experiments, does not influence the output of plasma proteins. Liver extract (parenteral) is also inert. The proteins of red blood cells when added to the diet are poorly utilized for plasma protein formation and show a potency ratio of only 10.1. Kidney protein added to the kidney basal diet shows a potency ratio of about 5 as compared with 4.6 for that basal diet. A digest of beef stomach and rice polishings shows a potency ratio of about 7.9. Dried powdered serum shows a potency ratio of 3.5, which is much less than fresh serum (2.6). Powdered thyroid fed in doses sufficient to accelerate body metabolism shows no distinct effect upon plasma protein production not attributable to the protein in the thyroid powder itself. Long periods (25 to 30 weeks) of plasma depletion and basal diet intake remove much protein from body fluids and tissues. Associated with this protein depletion the dog loses its appetite and may vomit some food. There is loss of hair, a tendency to skin ulceration, and a distinct lowering of resistance to infection. The plasma protein output may fall to fasting levels in spite of food intake sufficient to maintain weight. We believe this condition to be a deficiency state related to severe depletion of the essential protein matrix of the body cells.

scholarly journals CASEIN DIGESTS PARENTERALLY UTILIZED TO FORM BLOOD PLASMA PROTEIN

1941 ◽  
Vol 73 (6) ◽  
pp. 727-743 ◽  
Author(s):  
S. C. Madden ◽  
L. J. Zeldis ◽  
A. D. Hengerer ◽  
L. L. Miller ◽  
A. P. Rowe ◽  
...  
Keyword(s):  
Blood Plasma ◽  
Plasma Protein ◽  
Plasma Proteins ◽  
Protein Production ◽  
Basal Diet ◽  
Clinically Normal ◽  
Blood Plasma Proteins ◽  
Resistance To Infection ◽  
Protein Output ◽  
Uniform Plasma

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 uniform plasma protein production on a basal diet limited in protein. Such dogs are clinically normal but have a lowered resistance to infection and certain intoxications. Casein digests given by vein or subcutaneously to such plasma depleted dogs are effective in promoting abundant new plasma protein production. Casein digest L by vein is equivalent to whole liver of like protein equivalence by mouth. The ratio of new plasma protein production to protein intake is 20 to 25 per cent in both instances. Casein digest L by vein gives the same response in plasma protein output as the same digest by mouth. Protein digest X by vein requires addition of tryptophane and cysteine to be effective in plasma protein production. The added cysteine sulfur is more than 95 per cent retained by the dog. The speed of digest injection has no effect on its utilization, within the range tested. Casein digest L given by vein to non-depleted dogs is less well utilized than in dogs depleted of plasma protein.

scholarly journals BLOOD PLASMA PROTEIN REGENERATION CONTROLLED BY DIET

1935 ◽  
Vol 61 (2) ◽  
pp. 261-282 ◽  
Author(s):  
W. T. Pommerenke ◽  
H. B. Slavin ◽  
D. H. Kariher ◽  
G. H. Whipple
Keyword(s):  
Blood Plasma ◽  
Plasma Protein ◽  
Plasma Proteins ◽  
Protein Production ◽  
Protein A ◽  
Basal Diet ◽  
Food Protein ◽  
Potency Ratio ◽  
Health And Disease ◽  
Clinical Conditions

When blood plasma proteins are depleted by bleeding, with return of washed red cells (plasmapheresis) it is possible to bring the dog to a steady state of low plasma protein and uniform plasma protein production on a basal diet. Such dogs are excellent test subjects by which the potency of various diet factors for plasma protein regeneration can be measured. To regenerate plasma proteins in any significant amount the depleted dog requires food protein. Some proteins are very potent for new plasma protein production and others are utilized poorly. Beef serum is very potent and its proteins (2.6 gm.) will produce 1 gm. of new plasma protein in the depleted dog—a potency ratio of 2.6. Kidney protein stands at the bottom of our list and the dog needs 21 gm. of kidney protein to regenerate 1 gm. of plasma protein—a potency ratio of 21.0. Some grain proteins approximate the potency of beef serum and may show potency ratios of 2.7 to 4.6. Some of these grain proteins appear to favor the production of globulin more than albumin in the plasma. Skeletal muscle, gizzard (smooth muscle), lactalbumin and egg white fall into a favorable group with a potency ratio of 5.3 to 6.0. Whole liver, liver fractions, casein, and beef heart are a little less potent and present potency ratios of 6.5 to 8.0. Many of these food substances favor the production of albumin more than globulin. Pancreas and salmon muscle show less favorable potency ratios of 19.0 and 15.0 respectively. Fasting periods indicate that these depleted dogs can produce little if any new plasma protein. Iron feeding in some unexplained manner will influence body metabolism so that an excess of plasma protein will be produced. These observations have a bearing on clinical conditions associated with hypoproteinemia and give suggestions for diet aid or control in some of these abnormal states. The make-up of the diet is obviously of great interest and it is possible that protein combinations may be more potent than a single protein or that food potency ratios may differ in health and disease.

Blood plasma protein and lipid profile changes in calves during the first week of life

2013 ◽  
Vol 16 (3) ◽  
pp. 425-434 ◽  
Author(s):  
A. Herosimczyk ◽  
A. Lepczyński ◽  
M. Ożgo ◽  
A. Dratwa-Chałupnik ◽  
K. Michałek ◽  
...  
Keyword(s):  
Blood Plasma ◽  
Lipid Profile ◽  
Plasma Protein ◽  
Plasma Proteins ◽  
Postnatal Life ◽  
White Variety ◽  
Blood Plasma Protein ◽  
Apolipoprotein A ◽  
Peptide Mass ◽  
Profile Changes

Abstract The present study was undertaken to determine blood plasma protein and lipid profile changes in healthy Polish Holstein-Fresian calves of Black-and-White variety. Blood was drawn immediately after birth, before first colostrum intake and at the 3rd, 6th, 12th, 24th, 36th, 48th and 72nd hour of life. Subsequent four blood samples were collected at 24 hour intervals until the 7th day of life. Plasma proteins within the isoelectric point ranging from 3.0 to 10.0 were separated using high resolution two-dimensional electrophoresis. Among the 74 protein spots detected and analyzed, 16 were significantly altered during the first week of life. Differentially expressed spots were excised from the gels and subjected to peptide mass fingerprinting using MALDI-TOF MS. In total, 12 spots were successfully identified, which correspond to three proteins, namely: apolipoprotein A-I, apolipoprotein A-IV and fibrinogen gamma-B chain. A gradual increase in plasma triglyceride, total cholesterol, HDL and LDL cholesterol values was shown during the first seven days of calves life. The lowest concentration of these indicators were observed at birth and was followed by a rapid increase during the first week of postnatal life. These changes appear to be related to the transition in energy sources, from a maternal nutrient supply comprising mainly carbohydrates and amino acids to a diet which was rich in fat - colostrum and milk. This was reflected by the intense up-regulation of plasma proteins related with lipid transport and lipoprotein metabolism during the first week of life.

scholarly journals BLOOD PLASMA PROTEIN REGENERATION CONTROLLED BY DIET

1936 ◽  
Vol 63 (2) ◽  
pp. 277-301 ◽  
Author(s):  
J. B. McNaught ◽  
V. C. Scott ◽  
F. M. Woods ◽  
G. H. Whipple
Keyword(s):  
Blood Plasma ◽  
Plasma Protein ◽  
Plasma Proteins ◽  
Protein Production ◽  
Basal Diet ◽  
Sharp Drop ◽  
Bean Meal ◽  
Blood Plasma Proteins ◽  
Clinical Conditions ◽  
Uniform Plasma

When blood plasma proteins are depleted by bleeding, with return of washed red cells (plasmapheresis), it is possible to bring the dog to a steady state of low plasma protein in the circulation and a uniform plasma protein production on a basal diet. These dogs become test subjects by which the potency of various diet factors for plasma protein regeneration can be measured. Plant and grain proteins are quite well utilized to form new plasma protein in these test dogs but soy bean meal probably should be rated at the head of this list. It is utilized with unexpected promptness and favors the production of albumin in contrast to other plant proteins which distinctly favor globulin production. Long plasmapheresis periods on basal rations rich in grain proteins lower the resistance of these animals to infection. Spleen, brain, and stomach when fed with the basal diet in these test dogs show less favorable potency ratios—10.2, 11.8, and 13.6 respectively. This means the grams of tissue protein which must be fed to produce 1 gm. of new plasma protein. Fasting periods indicate that the dog can contribute only 4 to 6 gm. of plasma protein each week—an insignificant contribution presumably derived from the host's tissue proteins. Infection and intoxication disturb the plasma protein production of these standardized dogs and may reduce the output of plasma proteins to very low levels in spite of considerable food intake. There may be a very sharp drop in the plasma protein level during the first day of intoxication (Dog 33-324). Some of these observations may be of value in a study of clinical conditions associated with hypoproteinemia.

scholarly journals BLOOD PLASMA PROTEIN PRODUCTION AS INFLUENCED BY AMINO ACIDS

1939 ◽  
Vol 69 (5) ◽  
pp. 721-738 ◽  
Author(s):  
S. C. Madden ◽  
W. A. Noehren ◽  
G. S. Waraich ◽  
G. H. Whipple
Keyword(s):  
Blood Plasma ◽  
Red Blood Cells ◽  
Protein Content ◽  
Plasma Protein ◽  
Blood Cells ◽  
Plasma Proteins ◽  
Protein Production ◽  
Basal Diet ◽  
Liver Protein ◽  
Clinically Normal

When blood plasma proteins are depleted by bleeding with return of the washed red blood cells (plasmapheresis) it is possible to bring dogs to a steady state of hypoproteinemia and a uniform plasma protein production on a basal low protein diet. These dogs are clinically normal. By the introduction of variables into their standardized existence insight into the formation of plasma proteins can be obtained. The liver basal diet maintains health in such hypoproteinemic dogs during periods as long as a year. 17 to 27 per cent of its protein content (entirely liver protein) is presumably converted into plasma protein. Gelatin alone added to the liver basal diet causes very little if any extra plasma protein production. The addition to gelatin of cystine, or tyrosine, or tryptophane, or of both tyrosine and tryptophane has little or no effect on its potency for plasma protein production. When gelatin is supplemented by cystine and either tryptophane or tyrosine, 25 to 40 per cent of the protein content of the combination is converted into plasma protein—an efficiency equaling that of any protein hitherto tested. Preliminary experiments indicate that methionine cannot substitute for cystine nor can phenylalanine substitute for tyrosine in the efficient combination of gelatin plus cystine plus tyrosine. Laked red blood cells given by vein afford little or no material for plasma protein formation. When the reserve stores of plasma protein building material are exhausted the dog can form little if any plasma protein during protein-free diet periods.

scholarly journals Applicability of FTIR-ATR Method to Measure Carbonyls in Blood Plasma after Physical and Mental Stress

2019 ◽  
Vol 2019 ◽  
pp. 1-9 ◽  
Author(s):  
Jolanta Bujok ◽  
Marlena Gąsior-Głogowska ◽  
Michał Marszałek ◽  
Natalia Trochanowska-Pauk ◽  
František Zigo ◽  
...  
Keyword(s):  
Blood Plasma ◽  
Plasma Protein ◽  
Plasma Proteins ◽  
Antioxidant Defenses ◽  
Attenuated Total Reflectance ◽  
Oxygen Species ◽  
Carbonyl Groups ◽  
Combat Training ◽  
Horse Blood ◽  
Reflectance Ftir

Introduction. Oxidative stress is a state of imbalance between the production of reactive oxygen species and antioxidant defenses. It results in the oxidation of all cellular elements and, to a large extent, proteins, causing inter alia the formation of carbonyl groups in their structures. The study focused on assessment of changes in the plasma protein-bound carbonyls in police horses after combat training and after rest and the applicability of infrared spectroscopy with a Fourier transform, utilizing the attenuated total reflectance (FTIR-ATR) in detecting plasma protein oxidation. Methods. We evaluated the influence of both the different concentrations of hydrogen peroxide and combat training on protein carbonylation in horse blood plasma. The oxidation of plasma proteins was assessed using a spectrophotometric method based on the carbonyl groups derivatization with 2,4-dinitrophenylhydrazine (DNPH). The measured values were correlated with the carbonyl groups concentrations determined by means of the FTIR-ATR method. Results. The linear correlation between the DNPH and FTIR-ATR methods was shown. The concentration of plasma protein-bound carbonyls significantly deceased in police horses after one-day rest when compared to the values measured directly after the combat training (a drop by 23%, p<0.05 and 29%, p<0.01 measured by DNPH and FTIR-ATR methods, respectively). These results were consistent with the proteins phosphorylation analysis. Conclusion. The FTIR-ATR method may be applied to measure the level of plasma proteins peroxidation.

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