EFFECT OF TEMPERATURE AND PHOTOPERIOD ON THE SERUM PROTEINS OF THE RAINBOW TROUT, SALMO GAIRDNERI

1962 ◽  
Vol 40 (2) ◽  
pp. 127-130 ◽  
Author(s):  
Herman M. Meisner ◽  
C. P. Hickman Jr.
Keyword(s):  
Rainbow Trout ◽  
Serum Protein ◽  
Serum Proteins ◽  
Protein Pattern ◽  
Paper Electrophoresis ◽  
Effect Of Temperature ◽  
Salmo Gairdneri

The serum of 1- and 2-year-old rainbow trout, acclimated at least 43 days to four conditions of temperature and daylength (16°–8L (hours daily photoperiod), 16°–16L, 8°–8L, and 8°–16L) was examined by paper electrophoresis. The albumin/globulin ratio was significantly greater in trout acclimated to 8 °C (pooled photoperiod) than in those acclimated to 16 °C (pooled photoperiod). Photoperiod had no significant effect on the serum protein pattern.

scholarly journals Serum protein electrophoretic pattern in piglets during the early postnatal period

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Csilla Tóthová ◽  
Robert Link ◽  
Petronela Kyzeková ◽  
Oskar Nagy
Keyword(s):  
Serum Protein ◽  
Serum Proteins ◽  
Protein Pattern ◽  
Electrophoretic Pattern ◽  
Postnatal Period ◽  
Early Postnatal Period ◽  
Total Proteins ◽  
Newborn Piglets ◽  
Γ Globulins ◽  
Protein Electrophoretic Pattern

AbstractThe pattern of serum proteins, the typical features of the electrophoretogram in newborn piglets and during their postnatal development is not completely described. Therefore, the aim of this study was to characterize the changes in serum protein electrophoretic pattern and features of the electrophoretograms during the early postnatal period. Significant changes during the monitored period were found in all evaluated parameters (P < 0.001). The most marked changes were observed mainly in the period before weaning. The concentrations of total proteins, albumin and γ-globulins were before colostrum intake low, γ-globulins represented the smallest proportion of protein fractions. The proportion of α1-globulins was after birth a dominant protein fraction. Significant increase of total proteins, α2-, β- and γ-globulins and decrease of α1-globulins was found 2 days after colostrum intake. The albumin and A/G values increased after birth gradually until weaning. After weaning a significant changes were found in absolute concentrations of total protein and albumin, and in relative values of β-globulin fractions. Presented results showed marked developmental alterations in the serum protein pattern in piglets along with the age. The study also brings new knowledge in the field of description of typical features of electrophoretograms in the observed period of piglet’s life.

EFFECTS OF PORCINE IMMUNE GLOBULIN ADMINISTRATION ON THE SURVIVAL AND SERUM PROTEIN COMPOSITION OF COLOSTRUM-DEPRIVED PIGS REARED IN A NON-ISOLATED ENVIRONMENT

1961 ◽  
Vol 41 (2) ◽  
pp. 236-252 ◽  
Author(s):  
B. D. Owen ◽  
J. M. Bell ◽  
C. M. Williams ◽  
R. G. Oakes
Keyword(s):  
Oral Administration ◽  
Serum Protein ◽  
Immune Globulin ◽  
Serum Proteins ◽  
Protein Pattern ◽  
Post Partum ◽  
Protein Composition ◽  
Paper Strip ◽  
Percentage Survival ◽  
Immune Globulins

Five experiments involving 90 newborn colostrum-deprived pigs were conducted in an attempt to develop a method of rearing applicable in a non-isolated environment. Immune globulins, prepared by ammonium sulphate fractionation of porcine serum, and comprised of a mixture of approximately 75 per cent γ-globulin and 25 per cent β-globulin, were administered orally or parenterally in varying amounts and for varying periods of time. In two experiments porcine albumin, in serum or in a semi-purified solution, was provided in addition to the immune globulins. The distribution of serum proteins in the pigs was studied from birth to 12 weeks of age by paper strip electrophoresis.Parenteral administration of immune globulins did not provide an effective passive immunity, nor did oral administration for 1 day post-partum. A marked improvement in survival occurred when oral administration was continued for 5 days, and it was further found that this treatment provided apparently complete protection against infection during the 5-day period of administration. Albumin appeared to further improve survival.These results, together with the relatively poor survival obtained with positive control pigs (nursed 24 hours) suggested a continuing need for a supply of immune globulins in the lumen of the intestinal tract. Presumably these globulins were active as coproantibodies.The percentage survival in pigs weighing 3 pounds or more at birth was substantially higher than in smaller pigs. Mortality in these experiments was usually attributable to colibacillosis.Serum immune globulin levels at 2 days of age in the artificially reared pigs were elevated in proportion to the amount of globulins given. The effect of albumin was to create a serum protein pattern resembling that of suckled pigs. A marked decline in γ-globulin levels from 2 days to approximately 6 weeks was observed.

Diagnostic Effectiveness of Electrophoresis and Specific Protein Assays, Evaluated by Discriminate Analysis

1972 ◽  
Vol 18 (2) ◽  
pp. 116-123 ◽  
Author(s):  
Mario Werner ◽  
Samuel H Brooks ◽  
Georg Cohnen
Keyword(s):  
Multivariate Analysis ◽  
Clinical Diagnosis ◽  
Serum Protein ◽  
Protein Pattern ◽  
Paper Electrophoresis ◽  
Specific Protein ◽  
Discriminate Analysis ◽  
Disease Discrimination ◽  
Protein Assays

Abstract With use of the serum protein pattern as a model, we compared the "Diagnostic Effectiveness" of tests of different chemical specificity—i.e., the percentage classified correctly according to the clinical diagnosis. When results obtained from a selected population of subjects with selected diseases were evaluated by multivariate analysis, disease discrimination by paper electrophoresis, which resolves only chemically heterogeneous fractions, was similar to that of a battery of specific assays for individual proteins.

Effect of Temperature on Accumulation of Methylmercuric Chloride and p,p′DDT by Rainbow Trout (Salmo gairdneri)

1974 ◽  
Vol 31 (10) ◽  
pp. 1649-1652 ◽  
Author(s):  
Robert E. Reinert ◽  
Linda J. Stone ◽  
Wayne A. Willford
Keyword(s):  
Rainbow Trout ◽  
Water Temperature ◽  
Effect Of Temperature ◽  
Salmo Gairdneri ◽  
Methylmercuric Chloride ◽  
Concentration Factors

Amounts of mercury and DDT residues accumulated from water by yearling rainbow trout (Salmo gairdneri) in the laboratory increased as water temperature increased. Fish exposed to methylmercuric chloride at concentrations of 234–263 parts per trillion for 12 wk at 5, 10, and 15 C accumulated 1.19, 1.71, and 1.96 ppm; fish exposed to p,p′DDT at concentrations of 133–176 parts per trillion accumulated 3.76, 5.93, and 6.82 ppm. Concentrations of mercury accumulated by the fish were significantly different (P < 0.01) at each of the three temperatures, and the concentrations of DDT were significantly different at 5 and 10 and 5 and 15 C. Throughout the period of exposure, the concentration factors (concentration of contaminant in the fish/concentration in water) at each of the three temperatures were far higher for p,p′DDT than for methylmercuric chloride.

scholarly journals Studies in Bisalbuminemia: Binding Properties of the Two Albumins

Blood ◽  
1962 ◽  
Vol 20 (2) ◽  
pp. 156-164 ◽  
Author(s):  
EDWARD J. SARCIONE ◽  
C. WILLIAM AUNGST
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Protein ◽  
Serum Proteins ◽  
Protein Pattern ◽  
Total Serum ◽  
Binding Properties ◽  
Normal Human ◽  
Serum Components

Abstract 1. An abnormal serum protein pattern in a patient with Wegener’s granulomatosis and five of his relatives was identified as bisalbuminemia by electrophoretic and immunochemical methods. 2. With the exception of the patient with Wegener’s syndrome, the presence of bisalbuminemia was not associated with a significant change in total serum proteins, total albumin, serum components other than albumin, or any disease. 3. Addition of I131-thyroxine to bisalbumin sera resulted in thyroxine binding by albumin B but not by albumin A. The failure of albumin A to bind added I131-thyroxine leads to speculation that, in this family, neither albumin A nor B are identical to normal human serum albumin.

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