ZUR REGULATION DER PROTEINBIOSYNTHESE DURCH SEXUALHORMONE: DIE WIRKUNGEN VON OESTRADIOLBENZOAT UND VON TESTOSTERONPROPIONAT AUF DIE KONZENTRATION VON SERUMPROTEINEN

1970 ◽  
Vol 62 (2_Suppl) ◽  
pp. S9-S60 ◽  
Author(s):  
Alfred Oberdorfer
Keyword(s):  
Sex Hormones ◽  
Serum Protein ◽  
Laying Hens ◽  
Testosterone Propionate ◽  
Serum Proteins ◽  
Protein Biosynthesis ◽  
Total Serum Protein ◽  
Total Serum ◽  
Specific Gene ◽  
Protein Patterns

ABSTRACT Following intramuscular injections of oestradiol-17 β 3-monobenzoate and testosterone propionate in domestic fowl, typical alterations in the immunoelectrophoretic, starchgelelectrophoretic and ultracentrifugal patterns of serum proteins were observed. These effects are due to alterations in the concentrations of specific serum proteins. Both sex hormones alter the concentrations of the same proteins. The concentrations of various proteins are increased by one of the two hormones and decreased by the other. The administration of oestradiol-17β 3-monobenzoate alters the serum-protein patterns of pullets and immature cocks, nonlaying mature hens and mature cocks towards the pattern characteristic for laying hens. Testosterone propionate alters the pattern of serum proteins for laying hens towards the pattern that is characteristic for pullets and immature cocks, nonlaying mature hens and mature cocks. These alterations are reversible. Both the extent and the duration of the alterations are dependent upon the amounts of the hormones given. The results are discussed as being phenomena of hormonal effects on the biosynthesis of proteins. A comparison of the effects of the two sex hormones on the concentrations of total serum protein shows that in the case of oestradiol-17 β 3-monobenzoate the activating effects dominate. Testosterone propionate, however, seems to have more inhibitory effects than activating ones on the biosynthesis of proteins. On the basis of the theory advanced by Jacob & Monod, concerning the regulation of protein biosynthesis, and related to Karlson's hypothesis of gene activation, a model is proposed for a theoretical explanation of the results obtained here. It is assumed that both sex hormones, acting as effectors, influence the function of repressors with complementary structures and in this way activate or inactivate specific gene loci that are responsible for the biosynthesis of proteins.

Muscle Weight Relationship to Serum Proteins, Hemocytes, and Hepatopancreas in the Lobster, Homarus americanus

1967 ◽  
Vol 24 (11) ◽  
pp. 2339-2354 ◽  
Author(s):  
James E. Stewart ◽  
John W. Cornick ◽  
Diane M. Foley ◽  
M. F. Li ◽  
C. M. Bishop
Keyword(s):  
Serum Protein ◽  
Physiological Condition ◽  
Serum Proteins ◽  
Homarus Americanus ◽  
Total Serum Protein ◽  
Total Serum ◽  
Experimental Conditions ◽  
Muscle Weight ◽  
Beef Liver ◽  
The Relationship

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.

scholarly journals Serum proteinogram of the Campeiro horse

2019 ◽  
Vol 71 (2) ◽  
pp. 363-368
Author(s):  
A.F. Souza ◽  
J. Schade ◽  
A.F. Ramos ◽  
M.S.M. Albuquerque ◽  
G.V. Fonteque ◽  
...  
Keyword(s):  
Serum Protein ◽  
Serum Proteins ◽  
Reference Interval ◽  
Total Serum Protein ◽  
Total Serum ◽  
Serum Concentrations ◽  
Reproductive Condition ◽  
Serum Fractions ◽  
Pregnancy Status ◽  
Biuret Method

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.

Precipitation of serum proteins by the lectin from wheat-germ.

1987 ◽  
Vol 33 (1) ◽  
pp. 185-186 ◽  
Author(s):  
W E Schreiber ◽  
L Whitta
Keyword(s):  
Alkaline Phosphatase ◽  
Serum Protein ◽  
Wheat Germ ◽  
Serum Proteins ◽  
Total Serum Protein ◽  
Total Serum ◽  
Wheat Germ Lectin

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.

LEVELS AND PARTITION OF THE FOWL'S SERUM PROTEINS IN RELATION TO AGE AND EGG PRODUCTION

1955 ◽  
Vol 33 (1) ◽  
pp. 891-903 ◽  
Author(s):  
W. E. Vanstone ◽  
W. A. Maw ◽  
R. H. Common
Keyword(s):  
Serum Protein ◽  
Protein Level ◽  
Egg Production ◽  
Serum Proteins ◽  
Electrophoretic Pattern ◽  
Total Serum Protein ◽  
Total Serum ◽  
Zone Electrophoresis ◽  
Serum Protein Level ◽  
New Protein

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.

LEVELS AND PARTITION OF THE FOWL'S SERUM PROTEINS IN RELATION TO AGE AND EGG PRODUCTION

1955 ◽  
Vol 33 (6) ◽  
pp. 891-903 ◽  
Author(s):  
W. E. Vanstone ◽  
W. A. Maw ◽  
R. H. Common
Keyword(s):  
Serum Protein ◽  
Protein Level ◽  
Egg Production ◽  
Serum Proteins ◽  
Electrophoretic Pattern ◽  
Total Serum Protein ◽  
Total Serum ◽  
Zone Electrophoresis ◽  
Serum Protein Level ◽  
New Protein

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.

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
Keyword(s):  
Serum Protein ◽  
Half Life ◽  
Gamma Globulin ◽  
Serum Proteins ◽  
Growth Period ◽  
Unit Weight ◽  
Total Serum Protein ◽  
Total Serum ◽  
Beta Globulin ◽  
Newborn Animals

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.

scholarly journals Comparison of serum protein electrophoretic pattern in cows and small ruminants

2015 ◽  
Vol 84 (2) ◽  
pp. 187-195 ◽  
Author(s):  
Oskar Nagy ◽  
Csilla Tóthová ◽  
Veronika Nagyová ◽  
Gabriel Kováč
Keyword(s):  
Serum Protein ◽  
Adult Female ◽  
Serum Proteins ◽  
Electrophoretic Pattern ◽  
Small Ruminants ◽  
Protein Fractions ◽  
Total Serum Protein ◽  
Total Serum ◽  
Γ Globulins ◽  
Protein Electrophoretic Pattern

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.

Glomerular permselectivity to serum proteins in rainbow trout (Salmo gairdneri)

1988 ◽  
Vol 255 (3) ◽  
pp. R418-R423
Author(s):  
B. Elger ◽  
H. Ruhs ◽  
H. Hentschel
Keyword(s):  
Rainbow Trout ◽  
Glomerular Filtration ◽  
Serum Proteins ◽  
Salmo Gairdneri ◽  
Total Serum Protein ◽  
Total Serum ◽  
Protein Patterns ◽  
Gradient Gel Electrophoresis ◽  
Glomerular Hemodynamics

Changes in glomerular filtration rate (GFR) were induced in the unanesthetized rainbow trout by short-term adaptation from freshwater (FW) to brackish water (BW, 50% seawater) to investigate the effect of altered glomerular function on the glomerular permselectivity to endogenous serum proteins in vivo. Protein patterns of serum and urine were obtained by nondenaturing polyacrylamide gradient gel electrophoresis. In the serum, high-molecular-weight proteins dominate by 83.1 +/- 8.16%, and total serum protein concentrations were 3.25 +/- 0.32 (FW) and 3.12 +/- 0.16 g/100 ml (BW). The urinary protein concentration increased from 16.0 +/- 1.41 (FW) to 42.8 +/- 11.0 mg/100 ml (BW), whereas GFR and urine flow rate, both linearly related, decreased from 4.55 +/- 0.34 (FW) to 1.84 +/- 0.11 (BW) ml.h-1.kg-1 and from 2.31 +/- 0.19 (FW) to 0.56 +/- 0.02 (BW) ml.h-1.kg-1, respectively. The fractional clearance of protein increased exponentially at decreased GFR. This suggests increased glomerular filtration of serum proteins due to altered glomerular hemodynamics.

ELECTROPHORETIC ANALYSIS OF SERUM PROTEINS IN PREMATURE INFANTS

PEDIATRICS ◽  
1952 ◽  
Vol 10 (5) ◽  
pp. 527-532
Author(s):  
PATRICIA M. NORTON ◽  
HANS KUNZ ◽  
EDWARD L. PRATT
Keyword(s):  
Serum Protein ◽  
Premature Infants ◽  
Serum Proteins ◽  
Electrophoretic Analysis ◽  
Total Serum Protein ◽  
Total Serum ◽  
Gradual Decline

Forty-four measurements of the concentrations of total serum protein determined by a Kjeldahl procedure and of albumin, alpha 1, alpha 2, beta and gamma globulins determined electrophoretically in the serum of 27 premature infants ranging in age from 7 hours to 65 days are reported. Wide variations in all values are evident in individual cases. Certain trends are nevertheless apparent. During the first 5 to 6 weeks there is a gradual decline in the concentrations of total serum protein, albumin and gamma globulins. The alpha and beta globulins show no trend with age in this study. Except for slightly higher values for alpha 1 globulins in the smaller infants, none of the concentrations could be correlated with the birth weights of the patients.

Estimation of Serum Proteins by Electrophoresis on Cellulose Acetate

1972 ◽  
Vol 18 (12) ◽  
pp. 1541-1542 ◽  
Author(s):  
J W Keyser ◽  
G L Watkins
Keyword(s):  
Cellulose Acetate ◽  
Serum Protein ◽  
Serum Proteins ◽  
Standard Procedure ◽  
Total Serum Protein ◽  
Total Serum ◽  
Cellulose Acetate Electrophoresis ◽  
Ponceau S ◽  
Reference Serum ◽  
Electrophoresis Of Proteins

Abstract We have evaluated results for albumin obtained by a standard procedure for cellulose acetate electrophoresis of proteins in serum. The Ponceau S-stained albumin and globulins were eluted and the albumin was calculated by the generally accepted formula [(albumin-bound dye absorbance/absorbance of total protein-bound dye) x total serum protein concn] and by the formula (absorbance of albumin-bound dye in test/absorbance of albumin-bound dye in a reference serum) x concn of albumin in reference serum. The ratio of values by the first and second methods ranged from 0.93 to 1.30, the first giving the higher results in cases of discrepancy. These findings confirm the limitations in accurately calculating any serum-protein fraction by the first method. The second method appears to be the more accurate.

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