EFFECTS OF INFLAMMATION ON PROTEINS AND ENZYMES IN RAT PLASMA

1960 ◽  
Vol 38 (6) ◽  
pp. 575-584 ◽  
Author(s):  
S. W. Levy ◽  
de Guise Vaillancourt
Keyword(s):  
Plasma Proteins ◽  
Specific Activity ◽  
Rat Plasma ◽  
Limb Volume ◽  
Significant Change ◽  
Plasma Esterase

The effects of anaphylactoid inflammation in rats on the limb volume, hematocrit, and plasma proteins, and on the activities of plasmin, antiplasmin, and esterase of the plasma were studied. The hyperemia and edema of the limbs and other extremities which occurred following the injection of dextran were found to be accompanied by a transient hemoconcentration and a prolonged depression in the concentration of plasma proteins (both albumin and globulin fractions). The specific activity of plasma esterase was increased and that of antiplasmin was decreased during inflammation compared with control animals. No consistent or significant change was observed in the specific activity of plasmin.

EFFECTS OF INFLAMMATION ON PROTEINS AND ENZYMES IN RAT PLASMA

1960 ◽  
Vol 38 (1) ◽  
pp. 575-584 ◽  
Author(s):  
S. W. Levy ◽  
de Guise Vaillancourt
Keyword(s):  
Plasma Proteins ◽  
Specific Activity ◽  
Rat Plasma ◽  
Limb Volume ◽  
Significant Change ◽  
Plasma Esterase

The effects of anaphylactoid inflammation in rats on the limb volume, hematocrit, and plasma proteins, and on the activities of plasmin, antiplasmin, and esterase of the plasma were studied. The hyperemia and edema of the limbs and other extremities which occurred following the injection of dextran were found to be accompanied by a transient hemoconcentration and a prolonged depression in the concentration of plasma proteins (both albumin and globulin fractions). The specific activity of plasma esterase was increased and that of antiplasmin was decreased during inflammation compared with control animals. No consistent or significant change was observed in the specific activity of plasmin.

Binding of 5,5-Diphenylhydantoin and Its Major Metabolite to Human and Rat Plasma Proteins

1971 ◽  
Vol 60 (11) ◽  
pp. 1642-1646 ◽  
Author(s):  
Gordon J. Conard ◽  
Coryce O. Haavik ◽  
Kenneth F. Finger
Keyword(s):  
Plasma Proteins ◽  
Rat Plasma ◽  
Major Metabolite

THE INCORPORATION OF TRYPTOPHAN ANALOGUES INTO RAT PLASMA PROTEINS

1962 ◽  
Vol 40 (2) ◽  
pp. 153-157 ◽  
Author(s):  
Anita Berecz ◽  
C. Godin
Keyword(s):  
Plasma Proteins ◽  
Rat Plasma ◽  
Tryptophan Analogues

When 7-azatryptophan and 5-methyltryptophan are fed to protein-depleted rats, the animals lose weight more rapidly than control rats. Protein-depleted rats fed a diet containing tryptophan gain weight. 7-Azatryptophan is incorporated in vivo into rat plasma proteins, whereas 5-methyltryptophan is not incorporated.

Role of plasma lipids in transport of fatty acids for butterfat formation

1960 ◽  
Vol 198 (1) ◽  
pp. 45-47 ◽  
Author(s):  
P. M. Riis ◽  
Jack R. Luick ◽  
Max Kleiber
Keyword(s):  
Fatty Acids ◽  
Plasma Proteins ◽  
Turnover Rate ◽  
Plasma Lipids ◽  
Specific Activity ◽  
Plasma Lipid ◽  
Half Time

Cow plasma containing P32- and C14-labeled lipids and proteins was infused into a lactating cow. The specific activity of the lipids and volatile acids of the plasma and of the expired CO2 and milk constituents was determined. The turnover rate of phospholipid P and of plasma lipid volatile acids was 0.1 hours–1, this means a half-time of 7 hours. Little radioactivity was found in the expired CO2 and none was found in plasma volatile acids. These findings and the distribution of C14 in milk constituents indicate that plasma proteins do not contribute carbon to butterfat and that the catabolism of plasma lipids and proteins does not lead to a significant formation of nonlipid butterfat precursors. These observations permit a further calculation which indicates that 50% of the butterfat C originates from plasma lipid C.

scholarly journals Protein turnover in skeletal muscle of piglets

1974 ◽  
Vol 31 (1) ◽  
pp. 35-45 ◽  
Author(s):  
H. N. Perry
Keyword(s):  
Protein Turnover ◽  
Plasma Proteins ◽  
Hind Limb ◽  
Acid Metabolism ◽  
Specific Activity ◽  
Whole Body ◽  
Myofibrillar Proteins ◽  
Sarcoplasmic Proteins ◽  
Sarcoplasmic Protein ◽  
Suckling Piglets

1. Rates of protein synthesis and catabolism were measured in longissimus dorsi and hind-limb muscles of suckling piglets.2. Half-lives for synthesis and catabolism for mixed sarcoplasmic proteins were 4.8 and 9.4 d respectively. The corresponding values for mixed myofibrillar proteins were 5.7 and 16.4 d.3. The half-lives for synthesis of sarcoplasmic proteins were significantly different from those of myofibrillar proteins and were not confounded by contamination of the sarcoplasmic protein fraction with plasma proteins of higher specific activity.4. Individual myofibrillar proteins were synthesized and catabolized at rates which were not statistically significantly different. Intramuscular connective tissue also appeared to turnover rapidly, the half-life for synthesis being 8 d and that for catabolism 20 d.5. Values obtained for the specific radioactivities of aspartate + glutamate in mixed plasma proteins support the view that, in so far as the young of animals larger in mature body size than rats or mice are concerned, muscle assumes a more important role relative to liver in regulating whole body amino acid metabolism.

Determination of rat plasma esterase-1 (ES-1) activity by scanning densitometry of gradient polyacrylamide gels with zymogram detection

1991 ◽  
Vol 12 (12) ◽  
pp. 1045-1050 ◽  
Author(s):  
Hein A. Van Lith ◽  
Manuela Haller ◽  
Bert F. M. Van Zutphen ◽  
Anton C. Beynen
Keyword(s):  
Rat Plasma ◽  
Polyacrylamide Gels ◽  
Scanning Densitometry ◽  
Plasma Esterase

TURNOVER OF PLASMA GLUCOSE IN ANESTHETIZED WARM- AND COLD-ACCLIMATED RATS EXPOSED TO COLD

1959 ◽  
Vol 37 (2) ◽  
pp. 175-181 ◽  
Author(s):  
Florent Depocas
Keyword(s):  
Plasma Glucose ◽  
Specific Activity ◽  
Single Injection ◽  
Glucose Turnover ◽  
White Rats ◽  
Tracer Amount ◽  
Significant Change ◽  
Observation Period

The turnover of plasma glucose has been measured in anesthetized warm- and cold-acclimated white rats by a method involving a single injection of a tracer amount of uniformly labelled C14-glucose at 30 °C, and measurement of the rate of fall of the plasma glucose specific activity in animals maintained at 30 °C or moved to an environment at 6 °C. Analysis of the data indicated a significant increase in the rate of disappearance of the labelled glucose when the warm-acclimated rats were transferred from 30° to 6 °C but no significant change when the cold-acclimated rats were similarly treated. The concentration of plasma glucose remained essentially constant throughout the observation period. These results may be taken to indicate that the cold-induced increase in metabolism of anesthetized white rats is associated with an increase in plasma glucose turnover in warm-acclimated animals only.

Profiling of gender-specific rat plasma proteins associated with susceptibility or resistance to diet-induced obesity

2012 ◽  
Vol 75 (4) ◽  
pp. 1386-1400 ◽  
Author(s):  
Jung-Won Choi ◽  
Hao Liu ◽  
Duk Kwon Choi ◽  
Tae Seok Oh ◽  
Rajib Mukherjee ◽  
...  
Keyword(s):  
Plasma Proteins ◽  
Rat Plasma ◽  
Diet Induced Obesity ◽  
Gender Specific

Effect of physical training on the metabolism of thyroid hormones in man

1975 ◽  
Vol 38 (2) ◽  
pp. 212-215 ◽  
Author(s):  
A. Balsam ◽  
L. E. Leppo
Keyword(s):  
Physical Training ◽  
Plasma Proteins ◽  
Degradation Rate ◽  
Metabolic Clearance ◽  
Hormone Binding ◽  
Differential Impact ◽  
Before And After ◽  
The Absolute ◽  
Significant Change ◽  
Peripheral Metabolism

he effect of a 6-wk program of physical training (track running) on the peripheral metabolism of thyroxine (T4) and triiodothyronine (T3) was evaluated in a group of 11 men. Measurements were made of hormone turnover, urinay and fecal clearances, plasma hormone concentrations, and hormone binding by plasma proteins in all subjects before and after training, After training, metabolic clearance of T3 was increased 8.5% above the pretraining level due to an increased deiodinative clearance of this hormone. No significant change was observed in plasma T3 concentration. The absolute degradation of T3 increased 10.3% after training. In contrast, no significant change in the metabolic clearance of T4 was detected. Significantly decreased plasma concentration of total T4 after 4 and 6 wk of training was apparently not due to decreased hormone binding by plasma protein since no significant alteration in the dialyzable fraction of T4 was detected. The absolute degradation rate of T4 was decreased 8.8% after training. Possible implications of the observed differential impact of training on the degradation of T4 and T3 regarding thyroid hormone economy are discussed.

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