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At least 955 records · Page 53Linked to original sources

PubMed1978

Different expressions for enzyme activities in organs of rat. Application to aspartate transaminase, glutamate dehydrogenase and AMP-deaminase.

The widely used activity expressions for enzyme levels in tissues are discussed: microkatals per unit of tissue weight, protein weight, and DNA weight. The expression of microkatals present in a definite organ in reference to a standard animal weight, 100 g in the case of rat, is also used. The different expressions are applied to aspartate transaminase, glutamate dehydrogenase and AMP deaminase activities in liver, hind leg striated muscle and kidneys in rat. The conclusion is reached that measurements of enzyme activity in tissues should be expressed in more than one form, as the information drawn from one could differ substantially from that obtained from other, giving artifactual views of the metabolic role played by the enzyme in a given tissue.

Adenosine Deaminase↗

PubMed1981

[Effect of gene dose on cytoplasmic glutamate-oxaloacetate transaminase in embryonic mice with trisomy 19].

Trisomy for autosome No. 19 in mouse embryos (days 12-14 of development) was accompanied by a 1.5-fold increase in specific activity of cytoplasmic glutamate-oxaloacetate transaminase whose gene is known to be located in the 19th chromosome. Specific activity of cytoplasmic malate dehydrogenase remained unchanged under these circumstances, while activity of lactate dehydrogenase increased 1.1-fold.

Animals↗

PubMed1978

[Improved procedure for purification of aspartate transaminase from chicken heart cytosol. Characterization of the enzyme].

The purification procedure reported includes fractionation of water extract from chicken hearts with ammonium sulfate, fractional precipitation with ethanol, chromatography on Whatman CM-52 cellulose and crystallization. Specific activity of the pure crystalline enzyme was 234 micromoles.min-1.mg-1, as determined in the coupled assay with malate dehydrogenase (pH 7.5; 25 degrees). The amino acid composition of the enzyme was determined and the circular dichroism spectrum was recorded in the 200-250 nm range. The spectrum shows two negative bands with extrema at 208 and 220 nm. From the circular dichroism data it is estimated that aspartate transaminase contains approximately 40% alpha-helix and 10% beta-structure.

Amino Acids↗

PubMed1980

Effect of 24-hours fast on aspartate transaminase activities in the organs of the rat.

The aspartate transaminase activity of liver, kidney, brain, stomach, small intestine, striated muscle, skin and adipose tissue of fed and 24-hour fasted rats has been studied. The activity level of the enzyme is very much alike in most organs when expressed per unit of protein or DNA weight, in accordance with the general metabolic role of this enzyme. The activity of skin and adipose tissue is considerably lower than that of the other studied organs. A 24-hour fast induced significant increases in the activity of all organs except intestine and stomach.

Animals↗

PubMed1980

Glutamic oxaloacetic transaminase isozymes from rat liver. Purification and physicochemical characterization.

Glutamic oxaloacetic transaminase isozymes were purified simultaneously to homogeneity from rat liver with high yields. Three subforms of mitochondrial isozyme and three subforms of cytosolic isozyme were separated by chromatography on CM-Sephadex and electrophoresis on polyacrylamide gel. The general enzymatic properties of the purified isozymes such as their kinetic parameters, isoelectric points, molecular weights, amino acid compositions, NH2-terminal amino acid sequences and COOH-terminal amino acids were determined. Most of these properties of the isozymes are similar to those of the corresponding isozymes from other sources, such as rat brain and pig and human heart. In amino acid compositions, cytosolic isozyme from rat liver has more proline and glycine and less arginine, threonine and leucine than pig heart cytosolic isozyme; the mitochondrial isozyme has more glutamic acid and glycine and less serine than the corresponding pig heart isozyme. The NH2-terminal amino acid sequences of GOT isozymes from rat liver were identical with those of the GOT isozymes from pig heart up to the 10th residues except for the 5th residues. The subforms of mitochondrial isozyme from rat liver were generated on storage at 4 degrees C for 4-8 weeks.

Amino Acid Sequence↗

PubMedDate not supplied

[The extrathyroid effect of methylmercaptoimidazole. The effect of methylmercaptoimidazole on the isoenzyme distribution of tissue aspartate transaminase in thyroidectomized guinea pigs].

Administration of methylmercaptoimidazol to thyroidectomized guinea pigs decreased the activity and altered the isoenzymatic distribution of aspartic transaminase in the liver, myocardium and the brain tissue. The activity of the isoenzyme of the cytoplasm fell in all the three tissues under study. The activity of the isoenzyme of the mitochondria decreased in the liver, remained unchanged in the myocardium and increased in the brain tissue. The detected changes are associated with the direct action of methylmercaptoimidazol on the level of soluble cell proteins and on the energic metabolism in the mitochondria.

Animals↗

PubMed1997

Evaluation of aspartate transaminase activity and beta-hydroxybutyrate concentration in blood as tests for prediction of left displaced abomasum in dairy cows.

OBJECTIVE: To evaluate aspartate transaminase (AST) activity and beta-hydroxybutyrate (BHB) concentration in blood obtained during the first or second postpartum (PP) week as tests for prediction of subsequent left displaced abomasum (LDA) diagnosis in dairy cows. ANIMALS: 36 cows with LDA tested at a mean 3 PP days, which was 7 to 22 days prior to LDA diagnosis (25, 75% quantiles), and 28 cows with LDA tested at 10 PP days, which was 5 to 18 days prior to LDA diagnosis, were matched to 3 controls per case by herd and calving date. Data were available from a large field study. PROCEDURE: Odds ratio, sensitivity, specificity, and likelihood ratio were determined for various AST and BHB cutoff values. RESULTS: AST, using cutoff values between 100 and 180 U/L, and BHB, using cutoff values between 1,000 and 1,600 mumol/L, were significantly associated with subsequent LDA diagnosis. When cutoff values were increased, odds ratio and likelihood ratio increased; however, sensitivity decreased and specificity increased. CONCLUSION AND CLINICAL RELEVANCE: AST activity and BHB concentration in blood obtained during the first or second PP week might be useful as predictors of subsequent LDA diagnosis.

3-Hydroxybutyric Acid↗

PubMed1963