Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:2.6.1.2 (alanine aminotransferase)
26,722 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mitochondrial alanine aminotransferase L-alanine:2-oxoglutarate aminotransferase, EC 2.6.1.2) has been isolated in homogeneous form from both porcine liver and kidney cortex, but in low yield. Polyacrylamide gel electrophoresis of the purified enzyme in the presence of sodium dodecyl sulfate or 8 M urea gave a single band. An isoelectric point of 8.5 +/- 0.5 and a molecular weight of 75--80 000 were obtained. The enzyme is specific for L-alanine and is inhibited by D-alanine, aminooxyacetate and cyclosterine. The Km for pyruvate and glutamate is 0.4 mM and 32 mM, respectively. These values are similar to those determined for the cytoplasmic enzyme; however, at high concentrations, both compounds strongly inhibit the mitochondrial enzyme, an inhibition not observed with cytosolic alanine aminotransferase. These characteristics and the fact that the mitochondrial alanine aminotransferase was inactivated by procedures effective in the preparation of the cytosolic enzyme, clearly differentiate the two proteins and further support different roles for the two alanine aminotransferases in vivo.
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PMID:Isolation and characterization of mitochondrial alanine aminotransferase from porcine tissue. 45 16

Treatment of rats with cefazolin in vivo significantly suppressed activity of alanine and aspartate aminotransferases in serum and in the liver, brain, kidney, and heart. Simultaneous administration of pyridoxal further reduced enzyme activity except in the liver, where there was no change. Pyridoxal 5'-phosphate partly reversed the decreased enzyme activity in the serum, liver, and kidney, but did not return it to the amount observed in the control animals; enzyme activity remained suppressed in the brain and heart. The effect of cefazolin was dose related, but there was no sex-related difference. In contrast to its action on am-notransferase activity, cefazolin elicited no effect on alkaline phosphatase (pyridoxal-5'-phosphate hydrolase) in serum or on pyruvate carboxylase in the liver, heart, and kidney. Cefazolin exposed to the hepatic microsomal mixed-function oxidase system in vitro was partly converted into metabolites that inhibited serum alanine aminotransferase activity in vitro. The latter inhibition was reversed by the addition of pyridoxal 5'-phosphate.
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PMID:Decreased aminotransferase activity of serum and various tissues in the rat after cefazolin treatment. 45 47

After borohydride reduction, carboxymethylation, and tryptic digestion of the holoenzyme of pig heart alanine aminotransferase, a single icosapeptide containing the N6-(phosphopyridoxyl)lysine residue was isolated by a combination of gel filtration and ion-exchange chromatogrpahy. Its primary structure was determined as Gln-Glu-Leu-Ala-Ser-Phe-His-Ser-Val-Ser-Lsy(Pxy)-Gly-Phe-Met-Gly-Glu-Cys-Gly-Phe-Arg.
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PMID:Pyridoxal 5'-phosphate binding site of pig heart alanine aminotransferase. 46 50

Chronically alcoholized intoxication (1.5--2 months) induces adaptation of cerebral neurones to changing equilibrium states of biochemical processes by altering the activity of enzymes of GABA metabolism, reduction of alanine and aspartate transaminase activity and increase of LDH and succinate dehydrogenase activity. In the cerebellum and cerebral hemispheres during alcohol abstinacy the activity of GABA-T, succinate dehydrogenase and aspartate transaminase was reduced while that of LDH and alanine transaminase was increased. The administration of fusarinic acid (100 mg/kg i. p.) to control animals induced a sharp increase of GAD activity in both structures of the brain. The stimulatory effects of fusarinic acid were not observed when it was administered to animals receiving alcohol chronically. Motor activity or rats was markedly reduced during chronical alcoholism and the first days of alcohol abstinacy (24--48 h), as well as following injection fusarinic acid and homopantothenic acid. The increase of locomotion and the vertical component of motor activity was observed only following one week or one month after alcohol abstinacy.
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PMID:[Adaptive changes in brain metabolism during chronic alcoholic intoxication]. 57 38

Current belief that vitamin B6 deficiency causes depletion of muscle phosphorylase in animals appears to be erroneous. We present evidence that vitamin B6 deficiency is ineffective in reducing total phosphorylase in gasttocnemius muscle of young rats over a period of at least 8 weeks. Rats that had accumulated high levels of muscle phosphorylase while ingesting diets containing normal or excess amounts of the vitamin retained their phosphorylase after transfer to a vitamin B6 deficient diet. Prolonged deficiency did ultimately lead to enzyme depletion but this was after anorexia had developed and weight loss had occurred. When rats were partially starved for 1 to 4 days (fed 10% of normal energy intake) they lost muscle phosphorylase while retaining alanine and aspartate aminotransferases. When totally starved, the rats lost more phosphorylase than during partial starvation, but completely retained alanine aminotransferase, and lost some aspartate aminotrasferase. We conclude that the behavior of muscle phosphorylase is consistent with the Krebs-Fischer proposal that it acts as a reservoir for vitamin B6 and that starvation, but not vitamin B6 deficiency per se, causes depletion of muscle phosphorylase. It appears that phosphorylase may function as an adjunct ot adipose tissue necessary for the animal to efficiently meet the exigencies of starvation.
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PMID:The behavior of muscle phosphorylase as a reservoir for vitamin B6 in the rat. 63 54

The vitamin B6 status of Nigerian women, and the effects of three contraceptive methods--intrauterine contraceptive device, injectable progestogen, and combination estrogen-progestogen oral contraceptive pills--on the vitamin B6 status of these women were assessed by measuring the erythrocyte alanine aminotransferase (Ala-AT) activity both with and without in vitro stimulation by pyridoxal-5'-phosphate. The unstimulated Ala-AT activity and the Ala-AT index (ratio of pyridoxal-5'-phosphate-stimulated:unstimulated activity) were used as indications of vitamin B6 status. The criterion for vitamin B6 deficiency was an Ala-AT index greater than 1.25. Of the 238 women in the total sample, 11% were judged to be deficient. There were no significant differences in the mean Ala-AT activity, mean Ala-AT index or rate of deficiency foun in the control and three contraceptive groups. The absence of an effect of oral contraceptives on vitamin B6 status is in contrast with other cross-sectional studies, but in agreement with controlled longitudinal studies. The packed cell volume and reticulocyte count were also measured and were significantly affected by contraceptive steroids, but these effects are not thought to be of clinical importance.
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PMID:Vitamin B6 status of Nigerian women using various methods of contraception. 67 76

1. Diets containing graded levels of pyridoxine hydrochloride (to supply 0.26--30 mg pyridoxine/kg) were given to seven duplicate groups of turbot (Scophthalmus maximus) for 12 weeks and their growth rate was measured during this period. 2. Good growth was obtained on all treatments except those groups given less than 1.0 mg pyridoxine/kg diet. These fish grew normally until weeks 8--10 but thereafter their weight gain was significantly less than that for other treatments. 3. Measurements of aspartate aminotransferase (EC 2.6.1.1) in muscle and liver and of alanine amino-transferase (EC 2.6.1.2) in liver of the turbot showed that the activities of these enzymes increased with increasing dietary pyridoxine intake up to a level of 2.5 mg pyridoxine/kg. The activities of these enzymes were not further enhanced by additional dietary pyridoxine. 4. Percentage stimulation of these enzymes by pre-incubation of extracts with pyridoxal phosphate was minimal with those groups of turbot given 2.5 mg pyridoxine/kg diet or more. 5. It is concluded that the dietary requirement of turbot for vitamin B6 can be safely met with a diet containing between 1.0 and 2.5 mg pyridoxine/kg. 6. An eighth group of turbot given the pyridoxine antagonist 4-deoxypyridoxine hydrochloride (20 mg/kg) showed retarded growth after 2 weeks, together with a high mortality rate.
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PMID:Studies on the nutrition of marine flatfish. The pyridoxine requirement of turbot (Scophthalmus maximus). 69 64

Groups of Brahman-cross steers maintained on two nutritional planes were infected intravenously with a stabilate of Anaplasma marginale. In general, animals on the higher plane of nutrition were more severely affected. Fever was the first clinical sign of anaplasmosis but, like anaemia, was absent in the mildest cases. When present anaemia appeared two to three weeks after infection. There was a corresponding increase in erythrocyte sedimentation rates when read after 24 h but not at 1 h. The haemolytic nature of the anaemia was indicated by a significant increase in unconjugated bilirubin during the acute phase. Some visceral damage was suggested by a significant increase of serum aspartate amino-transferase (GOT) especially in severely affected animals of the 'high' nutrition group but no significant change occurred in levels of alanine amino-transferase (GPT).
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PMID:Experimental bovine anaplasmosis: clinico-pathological and nutritional studies. 70 52

The paper described the findings of the activity of aspartate amino transferase (GOT) and alanine amino transferase (GPT), lactate dehydrogenase (LDH), alkaline phosphatase (AP), and aldolase in the blood serum of calves examined for white-muscle disease (WMD). Relapsing mass accurrence of the disease was reported from various agricultural enterprises where calves were fed a milk replacer without vitamin E. In comparison with clinically healthy calves fed a feed mixture with vitamin E, calves suffering from the clinical form of WMD showed an alkaline phosphatase level decrease from 32.3 +/- 7.6 u. K. A. to 15.1 +/- 8.2 u. K. A. On the other hand, the activites of ALD, GOT, GPT, and LDH showed a statistically significant increase. The acute and sub-acute course of the disease increased enzyme activities as follows: ALD from 4.2 +/- 1.1 mumol (= 70.0 +/- 17.0 i.u.) to 9.7 +/- 2.1 mumol (= 163.0 +/- 33.2 i. u.), GOT from 0.9 +/-0.5 mumol (= 68.0 +/- 5.8 i.u.) to 16.7 +/- 11.7 mumol (= 567.0 +/-40.0 i. u.) GPT from 0.2 +/- 0.8 mumol (= 5.0 +/- 12.4 i. u.) to 9.8 +/- 2.8 mumol (= 330.0 +/- 40.4 i.u.), LDH from 46.1 +/- 5.4 mumol (= 765.0 +/- 40.0 i.u.) to 72.7 +/- 24.3 mumol (= 1,207.0 +/- 403.0 i.u.). In WMD-affected herds, similar enzyme activity fluctuations were observed even in calves showing no clinical signs of the disease. It follows from the study that the examination of serum enzymes provides a method to demonstrate the clinical and pre-clinical forms of white-muscle disease and that it can be included in the set of tests for the diagnosis of diseases in calves. The significant differences in all calves in the affected herds show that the disease is a danger to all animals in the herd fed a deficient mixture.
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PMID:[Activity of some serum enzymes in calves suffering from white muscle disease]. 81 57

The paper described the findings of the activity of aspartate amino transferase (GOT) and alanine amino transferase (GPT), lactate dehydrogenase (LDH), alkaline phosphatase (AP), and aldolase in the blood serum of calves examined for white-muscle disease (WMD). Relapsing mass accurrence of the disease was reported from various agricultural enterprises where calves were fed a milk replacer without vitamin E. In comparison with clinically healthy calves fed a feed mixture with vitamin E, calves suffering from the clinical form of WMD showed an alkaline phosphatase level decrease from 32.3 +/- 7.6 u. K. A. to 15.1 +/- 8.2 U. K. A. On the other hand, the activities of ALD, GOT, GPT, and LDH showed a statistically significant increase. The acute and subacute course of the disease increased enzyme activities as follows: ALD from 4.2 +/- 1.1 mumol (= 70.0 +/- 17.0 i. u.) to 9.7 +/- 2.1 mumol (= 163.0 +/- 33.2 i. u.), GOT from 0.9 +/- 0.5 mumol (= 68.0 +/- 5.8 i. u.) to 16.7 +/- 11.7 mumol (= 567.0 +/- 40.0 i. u.), GPT from 0.2 +/- 0.8 mumol (= 5.0 +/- 12.4 i. u.) to 9.8 +/- 2.8 mumol (= 330.0 +/- 40.4 i. u.), LDH from 46.1 +/- 5.4 mumol (= 765.0 +/- 40.0 i. u.) to 72.7 +/- 24.3 mumol (= 1,207.0 +/- 403.0 i. u.). In WMD-affected herds, similar enzyme activity fluctuations were observed even in calves showing no clinical signs of the disease. It follows from the study that the examination of serum enzymes provides a method to demonstrate the clinical and pre-clinical forms of white-muscle disease and that it can be included in the set of tests for the diagnosis of diseases in calves. The significant differences in all calves in the affected herds show that the disease is a danger to all animals in the herd fed a deficient mixture.
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PMID:[Activity of various serum enzymes in calves suffering from nutritionally-induced muscular dystrophy]. 81 73


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