scholarly journals The Metabolism of Serum Proteins in Neonatal Rabbits

1960 ◽  
Vol 43 (6) ◽  
pp. 1047-1059 ◽  
Author(s):  
Maria P. Deichmiller ◽  
Frank J. Dixon

1. Incorporation of S35-labeled amino acids into serum proteins has been studied in neonatal and developing rabbits. It was found that, per unit weight, neonatal rabbits synthesized only about 1/36 of the gamma globulin, 1/7 of the beta globulin, ½ of the alpha globulin, and ⅛ of the albumin that an adult synthesized. The growing rabbit developed the ability to synthesize various serum proteins at different times. 2. Plasma volumes and serum protein concentrations were determined at different times during the growth period of the rabbit. Plasma volumes were found to be 1 and ½ times larger in newborn animals than in adults, with a gradual decline to the adult level. The total serum protein concentration at birth was about 60 to 65 per cent of the adult value and gradually increased with growth as the plasma volume decreased. 3. Half-lives of homologous albumin and gamma globulin were studied. The half-life of albumin in neonates was nearly twice as long as the half-life in adults, the latter value being reached at 1 month of age. The half-life of gamma globulin in neonates was more than twice as long as the half-life in adults and reached adult values at 2 to 3 months. 4. Attempts were made to alter serum protein metabolism. Gamma globulin synthesis early in life was augmented with antigen injections.

1968 ◽  
Vol 48 (3) ◽  
pp. 415-424 ◽  
Author(s):  
A. G. Castell ◽  
J. P. Bowland

Pigs, from an experiment in which 0 and 0.10% supplemental CuSO4∙5H2O in diets were compared, were used to obtain information on the effects of supplementary copper on certain tissues. Blood hemoglobin values from weaning to market weight were not affected by the addition of supplemental copper. Serum copper levels were elevated in pigs receiving the copper-supplemented diet. This effect was most noticeable during the initial growth period up to 17 kg liveweight. Total serum protein and serum protein fractions were not consistently affected by dietary copper supplementation. Tissue copper levels in the liver, kidneys, heart, spleen, muscle and hair were obtained at different stages of growth. Comparative copper levels between pigs were variable, particularly for those pigs receiving the copper-supplemented ration, but distribution of copper between the tissues was relatively constant. The liver and kidneys were tissues which accumulated high levels of copper. Hair copper was increased when the dietary copper level was increased, but the heart, spleen and muscle had similar levels of copper in pigs fed either diet. The data suggest that during the early stages of growth there may be a metabolic requirement for copper above that normally available from the diet.


1967 ◽  
Vol 24 (11) ◽  
pp. 2339-2354 ◽  
Author(s):  
James E. Stewart ◽  
John W. Cornick ◽  
Diane M. Foley ◽  
M. F. Li ◽  
C. M. Bishop

Total serum protein values, hemocyte numbers, and muscle weights were determined for 216 intermolt lobsters immediately after their capture, and for 230 others held captive under a variety of dietary and environmental conditions. Average muscle values ranged from approximately 13% to the more normal 20–25% of the live animals' weight, depending upon experimental conditions. The total serum protein up to a level of 55 mg/ml was shown to be a reliable indicator of muscle weights, although the relationship was not identical for all lobster groups. It appeared to be modified chiefly by the areas from which the different groups were taken. Diet was more important than the temperatures (5 to 14 C) in affecting changes in muscle and serum protein values. Starvation caused a greater reduction (50 to 70%) in the size of the hepatopancreas than in the muscle. Histological examination of the hepatopancreatic tissue showed that the lipid content was markedly reduced upon starvation and that a degeneration of this organ was apparent for lobsters fed a beef liver and herring diet. Measurement of serum proteins would appear to be a useful technique in experiments on lobster nutrition and have value, within specified limits, for assessing the physiological condition of wild lobsters.


2019 ◽  
Vol 71 (2) ◽  
pp. 363-368
Author(s):  
A.F. Souza ◽  
J. Schade ◽  
A.F. Ramos ◽  
M.S.M. Albuquerque ◽  
G.V. Fonteque ◽  
...  

ABSTRACT The aim of this study to measure the fractions of the total serum proteins of the Campeiro horse and identify the influences of biological variants. Blood samples were taken in 138 horses of the breed Campeiro for measuring the concentration of total serum protein by the biuret method. Serum concentrations of protein fractions were measured by electrophoresis using agarose gel. Groups were formed according to age, sex and reproductive condition. The average values of serum fractions: albumin (2.85±0.36g/dl), alpha 1 (0.28±0.11g/dl), alpha 2 (0.26±0.08g/dL) beta 1 (0.57±0.15g/dl), beta 2 (0.89±0.28g/dL), gamaglobulinas (1.86±0.34g/dL), albumin/globulin ratio (0.75±0.18) and 2.5% percentile and 97.5% had slight differences in relation to the reference interval proposed for the species. They observed higher values of alpha 1 and 2 globulins in the group from that had six to eight years old and gammaglobulins in group above 13 years old. Serum protein concentrations were similar in horses and mares and between non-pregnant and pregnant. Sex and pregnancy status did not affect serum proteinogram. Alpha and gammaglobulins have higher values as the age increases. Serum proteinogram of Campeiro horses shows variations that have to be considered in the interpretation of laboratory tests.


1971 ◽  
Vol 17 (4) ◽  
pp. 301-306 ◽  
Author(s):  
John Savory ◽  
M Geraldine Heintges ◽  
Robert E Sobel

Abstract An automated continuous-flow procedure has been developed for simultaneously measuring total serum protein and globulin. The method for total protein is a minor modification of an existing automated method in which the biuret reagent is used. Total globulin is measured by reaction with glyoxylic acid, and standardized with N-acetyltryptophan. An empirical factor relating concentration of N-acetyltryptophan to human globulin has been derived. Values for total serum globulin obtained by this new automated procedure correlate closely with values obtained by electrophoresis, but do not agree with values obtained by use of procedures involving binding of anionic dye. Recovery of gamma globulin added to serum is essentially quantitative; the day-to-day precision (CV) is 4.31%.


1987 ◽  
Vol 33 (1) ◽  
pp. 185-186 ◽  
Author(s):  
W E Schreiber ◽  
L Whitta

Abstract We investigated the composition of the precipitate that forms when wheat-germ lectin derived from Triticum vulgaris is added to serum. A number of serum proteins are precipitated, representing about 2.5% of the total serum protein. This study demonstrates that the interaction of this lectin with the bone isoenzyme of alkaline phosphatase is not specific.


1955 ◽  
Vol 33 (1) ◽  
pp. 891-903 ◽  
Author(s):  
W. E. Vanstone ◽  
W. A. Maw ◽  
R. H. Common

The level of total serum protein in the fowl has been followed from the 14th day of incubation to the 13th week of egg production. Serum proteins have been fractionated concurrently by zone electrophoresis in filter paper. Serum protein level in the 14-day embryo was 0.9 gm./100 ml. and the protein comprised a prealbumin fraction, albumin, α2- and β-globnlins. Sera from chicks aged seven days no longer contained a prealbumin fraction but α1-,α3- and γ-globulin fractions had appeared by this stage and the protein level had reached 2.3 gm./100 ml. Total serum protein in females increased to a maximum of about 5.4 gm./100 ml. in the week before laying of the first egg. By that time two new protein fractions had appeared. These new fractions accounted for the greater part of the increase over the levels (4.0 gm./100 ml.) prevailing in the prepuberal stage. Serum protein level declined during the first three weeks of laying to average levels below 4.0 gm./100 ml.; and this decline appeared to affect albumin and α1-globulin as well as the new fractions. As laying progressed, the total serum protein tended to regain a level around 4.0 gm./100 ml. The electrophoretic pattern also tended to return towards that prevailing in the week before laying. Some tentative correlations of the results of zone electrophoresis with published results for free electrophoresis of fowl serum proteins are presented.


1963 ◽  
Vol 47 (2) ◽  
pp. 297-314 ◽  
Author(s):  
Jevrosima Radovich ◽  
Andor Szentivanyi ◽  
David W. Talmage

Homologous S35-labeled albumin, gamma globulin, and alpha-beta globulin were transfused into rabbits and the specific activities of the electrophoretic fractions of the sera of the recipients were determined at various time intervals up to 12 days after injection. Detectable reincorporation into a fraction other than that transfused was found only in the gamma globulin fraction after albumin injection. This activity rose between 2 and 12 days and reached a level of 2 to 3 per cent of the extrapolated zero time activity of the albumin fraction. When homologous serum protein doubly labeled with I131 and S35 was transfused into mice, marked drops in the ratios of I131 to S35 in the serum and tissue proteins were observed between 1 and 48 hours after injection. On the basis of a determination of the absolute and relative amounts of I131 and S35 found in the various tissue and serum proteins, the amount of reincorporation of S35 into each protein was calculated. The relative amounts of reincorporation of S35 among the various tissues were remarkably similar to the relative amounts of incorporation of S35 after the injection of labeled free amino acids. It is concluded that serum protein does not form a major direct source of amino acids to the tissues but feeds them indirectly through the extracellular pool.


1955 ◽  
Vol 33 (6) ◽  
pp. 891-903 ◽  
Author(s):  
W. E. Vanstone ◽  
W. A. Maw ◽  
R. H. Common

The level of total serum protein in the fowl has been followed from the 14th day of incubation to the 13th week of egg production. Serum proteins have been fractionated concurrently by zone electrophoresis in filter paper. Serum protein level in the 14-day embryo was 0.9 gm./100 ml. and the protein comprised a prealbumin fraction, albumin, α2- and β-globnlins. Sera from chicks aged seven days no longer contained a prealbumin fraction but α1-,α3- and γ-globulin fractions had appeared by this stage and the protein level had reached 2.3 gm./100 ml. Total serum protein in females increased to a maximum of about 5.4 gm./100 ml. in the week before laying of the first egg. By that time two new protein fractions had appeared. These new fractions accounted for the greater part of the increase over the levels (4.0 gm./100 ml.) prevailing in the prepuberal stage. Serum protein level declined during the first three weeks of laying to average levels below 4.0 gm./100 ml.; and this decline appeared to affect albumin and α1-globulin as well as the new fractions. As laying progressed, the total serum protein tended to regain a level around 4.0 gm./100 ml. The electrophoretic pattern also tended to return towards that prevailing in the week before laying. Some tentative correlations of the results of zone electrophoresis with published results for free electrophoresis of fowl serum proteins are presented.


2015 ◽  
Vol 84 (2) ◽  
pp. 187-195 ◽  
Author(s):  
Oskar Nagy ◽  
Csilla Tóthová ◽  
Veronika Nagyová ◽  
Gabriel Kováč

Determination of the physiological electrophoretic patterns in animals is very useful for clinicians in diagnosing healthy and sick animals. The objective of this study was to investigate the serum protein electrophoretic pattern in cows, sheep, and goats in order to evaluate the differences in the size and number of protein fractions between the evaluated ruminant species. Ten adult multiparous high-yielding dairy cows, 10 adult female sheep and 10 adult female goats were included in this study. All the evaluated animals were clinically healthy. Serum was analyzed for total serum protein concentrations, and for the relative and absolute values of protein fractions with calculation of albumin/globulin ratios. Serum protein fractions were separated by zone electrophoresis on buffered agarose gel. Serum protein electrophoresis identified 6 distinct bands, comprising albumin, alpha1- (α1), alpha2- (α2), beta1- (β1), beta2- (β2), and gamma- (γ) globulins in cows. In sheep, serum proteins exhibited 6 fractions: albumin, α1-, α2-, β-, γ1- and γ2-globulins. In goats, serum proteins were separated into 5 fractions: albumin, α1-, α2-, β- and γ-globulins. Significant differences in the relative as well as absolute means were found for the albumin/globulin ratio and most of the protein fractions, except γ-globulins. No significant differences were found in the concentration of total proteins. These results describe the marked species differences in most of serum protein fractions between the evaluated groups of animals, and contribute to the current knowledge about the physiological electrophoretic pattern of serum proteins in ruminants, which can be used for diagnostic purposes.


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