GLYCOLYTIC ENZYMES IN THE TISSUES OF A SALMONOID FISH (SALMO GAIRDNERII GAIRDNERII)

1963 ◽  
Vol 41 (1) ◽  
pp. 1971-1981 ◽  
Author(s):  
Robert A. MacLeod ◽  
R. E. E. Jonas ◽  
E. Roberts
Keyword(s):  
Skeletal Muscle ◽  
Heart Muscle ◽  
Lactic Dehydrogenase ◽  
Glycolytic Enzymes ◽  
The Other ◽  
Hexokinase Activity ◽  
Tissue Homogenates ◽  
Liver And Kidney ◽  
Free Glucose

Glycolysis in various tissues of the steelhead trout (Salmo gairdnerii gairdnerii) has been studied in vitro using tissue extracts and homogenates. Of the tissues examined, skeletal muscle, heart muscle, liver and kidney, only heart muscle homogenate was found to be capable of converting free glucose to lactic acid without added hexokinase. Low hexokinase activity or low hexokinase activity coupled with adenosine triphosphatase activity accounted for the failure of the other tissue homogenates to attack glucose.Qualitative and quantitative studies have indicated the presence of hexokinase, phosphoglucoisomerase, phosphofructokinase, aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphoglyceromutase, enolase, pyruvic kinase, and lactic dehydrogenase in the various fish tissues examined. Except for hexokinase and phosphofructokinase, the activities of the glycolytic enzymes of skeletal muscle were found to be 10 to 100 times greater than those of the same enzymes in the other tissues tested.Diphosphopyridine nucleotide (DPN) and adenosine diphosphopyridine (ADP) were cofactors and iodoacetate and fluoride plus phosphate inhibitors of enzymes of the fish glycolytic systems.It can be concluded from this study that the Embden–Meyerhof glycolytic pathway functions in tissues of the anadromous salmonoid S. gairdnerii gairdnerii.

GLYCOLYTIC ENZYMES IN THE TISSUES OF A SALMONOID FISH (SALMO GAIRDNERII GAIRDNERII)

1963 ◽  
Vol 41 (9) ◽  
pp. 1971-1981 ◽  
Author(s):  
Robert A. MacLeod ◽  
R. E. E. Jonas ◽  
E. Roberts
Keyword(s):  
Skeletal Muscle ◽  
Heart Muscle ◽  
Lactic Dehydrogenase ◽  
Glycolytic Enzymes ◽  
The Other ◽  
Hexokinase Activity ◽  
Tissue Homogenates ◽  
Liver And Kidney ◽  
Free Glucose

Glycolysis in various tissues of the steelhead trout (Salmo gairdnerii gairdnerii) has been studied in vitro using tissue extracts and homogenates. Of the tissues examined, skeletal muscle, heart muscle, liver and kidney, only heart muscle homogenate was found to be capable of converting free glucose to lactic acid without added hexokinase. Low hexokinase activity or low hexokinase activity coupled with adenosine triphosphatase activity accounted for the failure of the other tissue homogenates to attack glucose.Qualitative and quantitative studies have indicated the presence of hexokinase, phosphoglucoisomerase, phosphofructokinase, aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphoglyceromutase, enolase, pyruvic kinase, and lactic dehydrogenase in the various fish tissues examined. Except for hexokinase and phosphofructokinase, the activities of the glycolytic enzymes of skeletal muscle were found to be 10 to 100 times greater than those of the same enzymes in the other tissues tested.Diphosphopyridine nucleotide (DPN) and adenosine diphosphopyridine (ADP) were cofactors and iodoacetate and fluoride plus phosphate inhibitors of enzymes of the fish glycolytic systems.It can be concluded from this study that the Embden–Meyerhof glycolytic pathway functions in tissues of the anadromous salmonoid S. gairdnerii gairdnerii.

scholarly journals HISTOCHEMISTRY OF LACTIC DEHYDROGENASE IN HEART AND PECTORALIS MUSCLES OF RAT

1971 ◽  
Vol 51 (3) ◽  
pp. 621-635 ◽  
Author(s):  
Nobuhisa Baba ◽  
Hari M. Sharma
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Heart Muscle ◽  
Intracellular Localization ◽  
Pectoralis Major Muscle ◽  
Lactic Dehydrogenase ◽  
Left Ventricular ◽  
Ground Substance ◽  
Moderate Activity ◽  
Strong Reaction

Left-ventricular heart muscle and pectoralis major muscle of the rat were studied to determine the intracellular localization of lactic dehydrogenase (LDH) isoenzymes. Fixation of tissue for 2 hr in 2% buffered formaldehyde provided the best preservation of the ultrastructure and enzyme activity. Total LDH activity was found diffusely in the ground substance of the sarcoplasm and in the mitochondria of the heart muscle. In skeletal muscle a strong reaction was noted in the sarcoplasmic reticulum, and moderate activity was seen in the ground substance of the sarcoplasm and in the mitochondria. Differentiation of the isoenzymes of LDH was accomplished by addition of 4 M urea or application of heat. Heart-type isoenzymes were mainly localized in the mitochondria and sarcoplasm, whereas muscle-type isoenzymes were localized mainly in the sarcoplasmic reticulum of the skeletal muscle. It is speculated that the sarcoplasmic reticulum of the skeletal muscle is the site of anaerobic glycolysis and that the sarcoplasm and mitochondria are involved primarily in aerobic metabolism of pyruvate.

Post-natal growth and development of Simmental calves derived from in vivo or in vitro embryos

1998 ◽  
Vol 10 (6) ◽  
pp. 459 ◽  
Author(s):  
T. G. McEvoy ◽  
K. D. Sinclair ◽  
P. J. Broadbent ◽  
K. L. Goodhand ◽  
J. J. Robinson
Keyword(s):  
Growth And Development ◽  
The Other ◽  
Heart Weight ◽  
Post Mortem ◽  
Developmental Effects ◽  
Frozen Embryos ◽  
Liver And Kidney ◽  
Ad Libitum

Large fetuses arising from embryos produced in vitro have been shown to exhibit altered organ development in utero, but it is not known whether this persists post natally. Post-natal growth and development was examined in 18 Simmental bulls derived from in vivo frozen–thawed (n = 6), in vitro frozen– thawed (n = 6) or in vitro fresh (n = 6) embryos and reared together post weaning on an ad libitum diet until slaughter at approximately 13 months old. Calves weighing less than 60 kg at birth (n = 11) were classified as normal, and heavier calves (n = 7; all from in vitro embryos) as oversize. Lifetime growth rates and slaughter weights apparently were unaffected by embryo source or birthweight. Mean (± s.e.m.) post mortem liver and kidney weights were unaffected by embryo source, but hearts of bulls from in vitro frozen embryos were heavier than those of bulls from in vivo frozen embryos (2.7 ± 0.04 v. 2.3 ± 0.07 kg, P<0.025). Heart weight per kilogram body weight at slaughter for the 7 perinatally oversize males (4.01 ± 0.08 g) exceeded that of the other 5 bulls from in vitro embryos (3.60 ± 0.10 g kg −1 ; P<0.04) and the 6 in vivo males (3.56 ± 0.12 g kg −1 ; P<0.02). Overall, one-third of the variation in heart weight at slaughter (r 2 = 0.35; P = 0.01) was due to variation in birthweight. This is the first study to demonstrate birthweight-related developmental effects on post-natal organ weight following the transfer of embryos produced in vitro.

scholarly journals THE INDOPHENOLOXYDASE CONTENT OF TISSUES FROM RABBITS INFECTED WITH PNEUMOCOCCUS

1914 ◽  
Vol 19 (3) ◽  
pp. 303-308
Author(s):  
Florentin Medigreceanu
Keyword(s):  
Normal Control ◽  
Heart Muscle ◽  
Room Temperature ◽  
Renal Cortex ◽  
Pathological Change ◽  
Animal Cell ◽  
Liver And Kidney ◽  
Normal Controls ◽  
Rabbit Tissues

1. The action of indophenoloxydase is generally diminished in the tissues (liver, renal cortex, heart muscle) of rabbits that die of pneumococcus septicemia. The diminution is more frequent and marked in the liver and kidney than in the heart muscle. 2. The diminished activity of indophenoloxydase becomes more evident when the tissues undergo autolysis. At 37° C. this ferment is much more easily destroyed in the tissues of the infected animals than in those from normal control animals (tables I, II, III, and IV). Exceptions are rare and they occur chiefly with the heart muscle. 3. Normal rabbit tissues, inoculated in vitro with pneumococcus culture, do not lose their indophenoloxydase much more quickly than do the normal controls, when they are kept either at room temperature or at 37° C. (tables IV, V, VI, and VII). 4. It is therefore probable that the diminished activity of the indophenoloxydase of tissues from rabbits with pneumococcus septicemia is not due to the presence of the pneumococcus in these tissues, but that it is associated with a pathological change in the animal cell during life.

scholarly journals Leucine degradation in sheep

1988 ◽  
Vol 59 (2) ◽  
pp. 323-333 ◽  
Author(s):  
W. G. Bergen ◽  
J. R. Busboom ◽  
R. A. Merkel
Keyword(s):  
Skeletal Muscle ◽  
Adipose Tissue ◽  
Protein Intake ◽  
Crude Protein ◽  
Minor Role ◽  
Protein Nitrogen ◽  
Kidney Length ◽  
Tissue Homogenates ◽  
Leucine Catabolism

1. In vitro leucine catabolism in adipose tissue, skeletal muscle, kidney and liver homogenates was studied in sheep.2. In Expt 1, Suffolk × Targhee ram lambs were slaughtered at 1, 28, 56, 84, 112, 140, 168, 196, 224 and 365 d of age. In Expt 2, 5-month-old crossbred wethers were fed on 80, 120 or 180 g crude protein (nitrogen × 6·25) /kg diets for 4 weeks or fed on 120 g crude protein/kg for 4 weeks and then fasted for 48 or 96 h before slaughter. Leucine catabolism was assayed in tissue homogenates for Expts 1 and 2.3. Leucine deamination (per unit protein) was highest in skeletal muscle at day 1 and then declined; liver exhibited an activity pattern akin to muscle while kidney activity tended to rise over the duration of the study. Adipose tissue in vitro leucine deamination was higher at all ages studied and 9- to 50-fold higher than all other tissues at 365 d. Leucine decarboxylation (per unit protein) was highest at day 1 in muscle and declined to low levels (P < 0·01) after 28 d; liver and kidney decarboxylation activities were higher than muscle at all ages with kidney showing the highest activity. Whilst adipose had high initial activity it declined significantly (P < 0·01) by day 28 and remained low.4. Dietary protein intake had no effect on leucine deamination in any tissue. Leucine decarboxylation tended to increase with protein intake for all tissues except kidney. Length of fast (96 h) resulted in a variable decline in leucine deamination; leucine decarboxylation was significantly lower in kidney, liver and adipose tissue after a 96 h fast.5. When these in vitro enzyme activity results are related to questions concerning the role of skeletal muscle in leucine catabolism in sheep, the present findings indicate that in grown sheep, skeletal muscle has a small to moderate role in total body leucine deamination but plays a very minor role in leucine decarboxylation. Adipose tissue appears to be a major site of leucine deamination in grown sheep. These results are not in agreement with the idea that during fasting leucine becomes an important energy substrate and is oxidized in skeletal muscle as has been shown in rodents.

The Respiration of Pig Heart Muscle and Skeletal Muscle in vitro

2010 ◽  
Vol 18 (9) ◽  
pp. 709-716
Author(s):  
C. Hende ◽  
E. Muylle ◽  
W. Oyaert ◽  
P. Roose
Keyword(s):  
Skeletal Muscle ◽  
Heart Muscle

Cow red blood cells. I. Effect of purines, pyrimidines, and nucleosides in bovine red cell glycolysis

1979 ◽  
Vol 236 (5) ◽  
pp. C255-C261 ◽  
Author(s):  
M. J. Seider ◽  
H. D. Kim
Keyword(s):  
Pyruvate Kinase ◽  
Enzyme Activities ◽  
Blood Cells ◽  
Glycolytic Enzyme ◽  
Red Cells ◽  
The Other ◽  
Red Cell ◽  
Hexokinase Activity ◽  
Glycolytic Rate

Cow red cells, under in vitro incubation conditions, exhibit a comparatively low glycolytic rate of 0.56 +/- 0.05 micromol/(ml cells.h), with a ratio of lactate formed to glucose consumed of 1.58. It has been found that this low glycolytic rate can be stimulated 50--60% above the basal level in the presence of a variety of purine and pyrimidine compounds including adenosine, inosine, adenine, hypoxanthine, xanthine, and uracil. In contrast, calf red cells, which have a much higher glycolytic rate, display no discernible response to these agents. In attempts to elucidate the mechanism by which this stimulation takes place, both glucose transport and glycolytic enzyme activities were determined in the presence of these stimulators. Glucose influx in cow red cells, measured using the glucose analog 3-O-methyl-glucose, exhibits both a low Km of 117 microM and a Vmax of 0.38 micromol/(ml cells.min), and is unaltered in the presence of adenosine. On the other hand, hexokinase, which in normal hemolysates of cow red cells has an activity of 0.49 +/- 0.03 micromol/(g Hb.min). was found to be stimulated to 0.73 micromol/(g Hb.min) in the presence of adenine. Both pyruvate kinase and phosphofructokinase were unaffected by this compound. These data suggest that certain purines and pyrimidine compounds may exert their stimulatory effect on hexokinase activity, resulting in an augmentation of cow red cell glycolysis.

scholarly journals A Pharmacokinetic and Pharmacodynamic Evaluation of the Anti-Hepatocellular Carcinoma Compound 4-N-Carbobenzoxy-gemcitabine (Cbz-dFdC)

Molecules ◽  
2020 ◽  
Vol 25 (9) ◽  
pp. 2218
Author(s):  
Yilin Sun ◽  
Jiankun Wang ◽  
Kun Hao
Keyword(s):  
Human Liver ◽  
Antitumor Effect ◽  
Intragastric Administration ◽  
Enzyme Kinetic ◽  
Tumor Bearing ◽  
Tissue Homogenates ◽  
Liver And Kidney ◽  
Carboxylesterase 1

Gemcitabine (dFdC) demonstrates significant effectiveness against solid tumors in vitro and in vivo; however, its clinical application is limited because it tends to easily undergo deamination metabolism. Therefore, we synthesized 4-N-carbobenzoxy-gemcitabine (Cbz-dFdC) as a lead prodrug and conducted a detailed pharmacokinetic, metabolic, and pharmacodynamic evaluation. After intragastric Cbz-dFdC administration, the Cmax of Cbz-dFdC and dFdC was 451.1 ± 106.7 and 1656.3 ± 431.5 ng/mL, respectively. The Tmax of Cbz-dFdC and dFdC was 2 and 4 h, respectively. After intragastric administration of Cbz-dFdC, this compound was mainly distributed in the intestine due to low carboxylesterase-1 (CES1) activity. Cbz-dFdC is activated by CES1 in both humans and rats. The enzyme kinetic curves were well fitted by the Michaelis–Menten equation in rats’ blood, plasma, and tissue homogenates and S9 of the liver and kidney, as well as human liver S9 and CES1 recombinase. The pharmacodynamic results showed that the Cbz-dFdC have a good antitumor effect in the HepG2 cell and in tumor-bearing mice, respectively. In general, Cbz-dFdC has good pharmaceutical characteristics and is therefore a good candidate for a potential prodrug.

Effect of starvation on initiation of protein synthesis in skeletal muscle and heart.

1978 ◽  
Vol 235 (2) ◽  
pp. E126 ◽  
Author(s):  
D E Rannels ◽  
A E Pegg ◽  
S R Rannels ◽  
L S Jefferson
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Heart Muscle ◽  
Psoas Muscle ◽  
Peptide Chain ◽  
Initiation Factor ◽  
Ribosomal Subunits ◽  
Chain Initiation ◽  
Rate Limiting

Psoas muscle of rats starved for 2 or 4 days contained increased levels of ribosomal subunits and exhibited reduced rates of protein synthesis in vitro, demonstrating a starvation-induced inhibition of peptide-chain initiation. The activity of an eIF-2-like initiation factor, assayed in postribosomal supernatants, decreased in psoas during starvation, parallel to a 25% reduction in the RNA level. Reduced eIF-2 activity did not result from nucleotide depletion or increased deacylation of initiator tRNA, nor was it abolished by extensive dialysis. Perfusion of psoas muscle in the presence of insulin reversed the starvation-induced block in peptide-chain initiation, but did not alter the activity of eIF-2 or level of RNA. Furthermore, heart muscle did not manifest a starvation-induced block in peptide-chain initiation even though the activity of eIF-2 and the level of RNA decreased as a result of food deprivation. Thus loss of eIF 2 activity in psoas and heart did not parallel changes in peptide-chain initiation but was associated with a reduction in tissue RNA. These results indicate that the level of eIF-2 is not rate-limiting for peptide-chain initiation under the conditions tested in this study.

Tissue and Bacterial Splitting of Sulphasalazine

1983 ◽  
Vol 64 (3) ◽  
pp. 349-354 ◽  
Author(s):  
A. K. Azad Khan ◽  
Glynis Guthrie ◽  
H. H. Johnston ◽  
S. C. Truelove ◽  
D. H. Williamson
Keyword(s):  
Azo Dyes ◽  
Enzyme System ◽  
Reductase Activity ◽  
Maximum Activity ◽  
The Other ◽  
Optimum Conditions ◽  
Anaerobic Conditions ◽  
Azo Reductase ◽  
Tissue Homogenates

1. The cleavage of sulphasalazine at the azo bond by bacterial suspensions and tissue homogenates has been studied in vitro. 2. For maximum activity the azo reductase system requires anaerobic conditions and the presence of cofactors, namely NADPH and FAD. in this respect, sulphasalazine resembles other azo dyes. 3. Under optimum conditions all the species of bacteria tested were capable of splitting sulphasalazine and there were no major differences in the degree of activity shown by different species. The enzyme system is located within the bacterial cell and does not leak out of it. 4. All the tissues tested, both human and rat, showed azo reductase activity. The liver showed a much higher activity than the other tissues.

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