Effect of mercuric chloride on serum protein catabolism and protein content of rabbit kidney

1962 ◽  
Vol 202 (6) ◽  
pp. 1121-1124 ◽  
Author(s):  
Lawrence I. Gottlieb ◽  
Robert D. Coye
Keyword(s):  
Protein Content ◽  
Serum Protein ◽  
Mercuric Chloride ◽  
Rabbit Kidney ◽  
Protein Catabolism ◽  
Major Site ◽  
Protein Label ◽  
Perfused Kidney

No effect of HgCl2 poisoning on the catabolism of serum protein was noted in rabbits in which I131 was used as the protein label. The amount of I131 remaining in the perfused kidney was much greater in the poisoned animals than in the controls. This increase in label was shown to be due to an increase in the protein. Using T-1824, smaller increases were noted in the poisoned kidneys. The data are interpreted to show that the kidney is not a major site of serum protein catabolism and that the increased protein in the kidney results from increased filtration through a damaged glomerular membrane.

Differential effects of methylmercuric chloride and mercuric chloride on the L-glutamate and potassium evoked release of [3H]dopamine from mouse striatal slices

1986 ◽  
Vol 64 (5) ◽  
pp. 656-660 ◽  
Author(s):  
S. J. McKay ◽  
J. N. Reynolds ◽  
W. J. Racz
Keyword(s):  
Calcium Channel ◽  
Glutamate Receptor ◽  
Mercuric Chloride ◽  
Neurotransmitter Release ◽  
Mechanisms Of Action ◽  
Major Site ◽  
Striatal Slices ◽  
Differential Effects ◽  
Methylmercuric Chloride ◽  
Site Of Action

The effects of CH3HgCl and HgCl2 on the evoked release of 3H from mouse striatal slices prelabelled with [3H]dopamine have been examined. CH3HgCl (10 μM) was observed to increase the L-glutamate-evoked release of [3H]dopamine, while HgCl2 (10 μM) had no effect. In contrast, CH3HgCl at concentrations up to 100 μM had no effect on the 25 mM K+-stimulated release of [3H]dopamine, whereas HgCl2 (100 μM) significantly reduced the 25 mM K+-stimulated release of [3H]dopamine. Thus CH3HgCl and HgCl2 have differential effects on the L-glutamate- and K+-stimulated release of [3H]dopamine from mouse striatal slices, suggesting that these compounds may have different sites and (or) mechanisms of action in altering neurotransmitter release. It is suggested that CH3HgCl may act predominantly at intracellular sites or at the level of the L-glutamate receptor, whereas the major site of action of HgCl2 may be the voltage-operated calcium channel.

Evaluation of Automated Dye Binding Determination of Protein in Milk

1974 ◽  
Vol 57 (1) ◽  
pp. 42-47
Author(s):  
Douglas L Park ◽  
Raymond L King
Keyword(s):  
Protein Content ◽  
Mercuric Chloride ◽  
Sampling Rate ◽  
Protein Determination ◽  
Binding System ◽  
Milk Samples ◽  
Instrument Performance ◽  
Dye Binding ◽  
Herd Milk

Abstract The Technicon AutoAnalyzer dye binding system for protein determination in milk was compared with the Kjeldahl and Udy methods. Individual cow and mixed herd milk samples were analyzed, including such variables as the effect of aging, chemical preservation, laboratory manipulation of protein content, and experimental changes in instrumental parameters. The Udy and Kjeldahl methods showed better agreement than the Technicon procedure in all treatments. Aging resulted in slight decreases in apparent protein content by both dye binding methods. Variation due to treatment with formaldehyde and mercuric chloride was considerable for the Technicon system (+ 0.72 and +0.20% protein, respectively). Individual cow milks varied more than herd milks and Guernsey more than Holstein milk. Milk samples standardized for protein content showed a high correlation with the Kjeldahl results. Replication by the Technicon system was superior to both the Udy and Kjeldahl methods. Performance of the Technicon system improved with increased dialyzing time, decreased dye concentration, and decreased sampling rate. Instrument performance was also influenced by dialysis membrance replacement.

scholarly journals Effect of the protein content of the diet on the vitamin B12 status in rats

1974 ◽  
Vol 31 (2) ◽  
pp. 219-225
Author(s):  
V. S. Jathar ◽  
R. S. Satoskar ◽  
B. M. Mehta ◽  
D. V. Rege
Keyword(s):  
Vitamin B12 ◽  
Protein Content ◽  
Serum Protein ◽  
Vitamin B ◽  
Tissue Binding ◽  
Fresh Weight ◽  
Protein Starvation ◽  
Nitrogen Contents ◽  
Total Tissue

1. The effects of the protein content of the diet on the vitamin B12 concentration of serum and of various tissues were studied in rats by means of microbiological and radioisotopic techniques.2. Protein starvation reduced tissue weights and nitrogen contents, serum protein concentrations and haemoglobin values.3. The vitamin B12 contents of the serum and of several organs and tissues were greater in the protein-starved animals for reasons that remain unexplained.4. The retention of radioactive cyanocobalamin per g fresh weight was significantly greater in liver, kidney, spleen and brain in the protein-depleted rats than in those given adequate protein. However, the total tissue retention was not significantly different between these groups, so that there was a greater capacity for tissue binding and for body conservation of vitamin B12 in the protein-starved animals.

PARALLEL STUDIES OF COMPLEMENT AND COAGULATION III. THE EFFECT OF THE PROTEIN LEVEL OF THE DIET

1951 ◽  
Vol 29 (1) ◽  
pp. 13-24
Author(s):  
Christine E. Rice ◽  
Paul Boulanger ◽  
P. J. G. Plummer
Keyword(s):  
Protein Content ◽  
Serum Protein ◽  
Total Protein ◽  
Protein Level ◽  
Guinea Pigs ◽  
Total Protein Content ◽  
Coagulation Time ◽  
Complement Components ◽  
The Mean ◽  
Protein Diets

The complement and coagulative activities of the blood were studied in three groups of 20 guinea pigs each, receiving diets containing different amounts of protein, 2.3 to 26.7%. The mean complement titers were found to be lower and the prothrombin times longer in the group fed the diet containing the least protein, 2.3%. Of the four major complement components,,the fourth, C'4, appeared to be most affected. Sera of the animals receiving less protein were lower in total protein content and had lower albumin - globulin ratios than sera from guinea pigs on the higher protein diets. No relationship was demonstrated between coagulation time and serum protein content.

scholarly journals EFFECTS OF LARGE INFUSIONS OF HETEROLOGOUS SERUM PROTEINS ON THE SERUM PROTEIN METABOLISM OF RABBITS

1955 ◽  
Vol 101 (3) ◽  
pp. 233-244 ◽  
Author(s):  
Frank J. Dixon ◽  
Paul H. Maurer
Keyword(s):  
Protein Synthesis ◽  
Serum Protein ◽  
Plasma Protein ◽  
Protein Metabolism ◽  
Serum Proteins ◽  
Foreign Protein ◽  
Protein Catabolism ◽  
Homologous Proteins ◽  
Protein Pool ◽  
Heterologous Serum

Infusions of heterologous serum proteins large enough to replace the entire normal catabolic loss of the corresponding autologous proteins in the recipient rabbits caused increased rates of plasma protein catabolism, an increase in the size of the plasma protein pool and normal or even slightly increased rates of plasma protein synthesis. The principal proteins in these infusions were catabolized at rates similar to those for corresponding homologous proteins. The most marked hyperproteinemias which developed were caused principally by increases in the host's own globulin and to a lesser extent by the presence of foreign protein in the circulation.

scholarly journals THE INFLUENCE OF DIET UPON THE REGENERATION OF SERUM PROTEIN

1936 ◽  
Vol 64 (6) ◽  
pp. 897-920 ◽  
Author(s):  
Daniel Melnick ◽  
George R. Cowgill ◽  
Ethel Burack
Keyword(s):  
Serum Protein ◽  
Protein Concentration ◽  
Dietary Factors ◽  
Experimental Production ◽  
Protein Catabolism ◽  
Fasting Period ◽  
Potency Ratio ◽  
Tissue Protein ◽  
Protein Free Diet ◽  
Serum Protein Concentration

1. By the technique of quantitative plasmapheresis the effects of single proteins in artificial synthetic diets were studied with respect to their value in promoting the regeneration of serum protein. 2. The ratio of (a) the amount of serum protein per week removed by bleeding above that regenerated by the dog when eating the protein-free diet, to (b) the dietary protein increment (i.e., above that required for nitrogen equilibrium) was termed the potency ratio. The results indicated that serum protein was slightly superior to casein and lactalbumin in promoting the regeneration of serum protein. However, the respective potency ratios, varying from approximately 0.51 to 0.36, were comparable and not widely divergent as those reported by others. It was concluded that, whereas in some individuals dietary proteins may be able to produce a significant increase in the serum protein concentration, the potency ratios are not sufficiently different to warrant the administration of any one protein in preference to another. 3. The inhibitory effect of the basal protein-free diet with respect to serum protein regeneration in the dog was also demonstrated by the inability of the protein concentration to attain the normal level in spite of discontinued plasmapheresis. However, a subsequent fasting period resulted in a progressive rise in the serum protein concentration until the normal value was approximated. These observations are interpreted as indicating that the products of tissue protein catabolism can be utilized in the formation of new serum protein. 4. The experimental production of what seems to be an inhibition of the serum protein regenerating mechanism was described. This observation together with the hypothetical evidence presented by Bloomfield (17) and Weech and his associates (9) suggests that the most profitable line of approach to solution of the problem of hypoproteinemia lies not so much in the evaluation of dietary factors but in finding a way for stimulating internally the serum protein regenerating mechanism, which seems to involve in some manner the capacity of the tissue to furnish protein for the needs of the plasma. 5. A hypothesis explaining the mechanisms responsible for serum protein formation was presented and the experimental support for it discussed. The rôle of tissue protein catabolism in this function was emphasized.

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