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)

The serum enzyme values (GOT, GPT, LDH and Aldolase) of 13 fit healthy volunteers were determined before and after physical effort of a moderate grade of 3.9 Kcal/min. The pulse rate pattern of the subjects during the exercise of climbing up and down a staircase for 30 minutes and during a 10 minute recovery phase was also recorded. The pulse pattern was in no case in excess of 150 bpm and full recovery was achieved within 10 minutes indicating that the exercise was moderate. The serum enzyme values after the exercise were raised. The difference between the exercise and rest values of the four enzyme activities were significant at the 1% level. It was observed that the raised enzyme activity level dropped to normal levels within 24 hours after the exercise. Large individual variations in the rise of these enzyme levels after exercise were observed and hence it is difficult to quantitate the phenomenon. Consequently the value of serum enzyme levels after the exercise as a practical-index of physiological strain is limited.
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PMID:Exercise induced serum enzyme changes in untrained subjects. 61 98

A 55-year-old female was admitted to our hospital because of high fever, nonproductive cough and dyspnea. Initially she had been treated with cephem antibiotics by a local doctor. However, acute respiratory failure due to severe pneumonia developed. The partial pressure of oxygen in arterial blood was 55.5 Torr. Her chest X-ray revealed wide-spread infiltrates with air bronchograms throughout the entire left lung, and pleural effusions were also present in the chest CT scan. Because the patient had a history of the contact with birds, we suspected psittacosis and administered Minocycline immediately. As a result, her clinical condition improved and the abnormal shadow on the chest X-ray film improved markedly in three days. Because the serum titer of a complement fixation test against Chlamydia rose to 1:512, we made the diagnosis of psittacosis. In addition, femoral muscle pain, and a high level of serum GOT, GPT, CK, Aldolase and Myoglobin indicated hepatitis and myositis. In the lung tissue specimens obtained by TBLB performed on the 10th hospital day, slight interstitial pneumonia and intracellular inclusion bodies were found by light microscopy and Chlamydial agents were found electron microscopically.
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PMID:[A case of fulminant psittacosis showing Chlamydia in TBLB specimens]. 204 Dec 51

This study was prompted by the paradox of strong presence of mitochondria in an anaerobic protozoan, recently reclassified from the yeasts. Stemming from publication in 1911 to 1912, Blastocystis hominis has been generally accepted as a harmless intestinal yeast of humans, with short standardized textbook (parasitology) descriptions, even to the present day. Reports since 1967 have changed the classification of B. hominis from yeast to protozoan (Sarcodina), and this has been followed by interest in B. hominis-caused disease, resulting in documentation of disease in humans and other primates. In this study of B. hominis, the basic ultrastructure of the mitochondria was shown by thin-section electron microscopy to be identical to that of an archetypical mitochondrion. There were hundreds of them in large B. hominis cells (100 to 200 microns in diameter). Mitochondria were confined to a peripheral ring of cytoplasm bounded by the outer cell membrane (there is no cell wall) and the membrane of the large, spherical, organelle-free central body that constitutes 75% of the cell's volume. Mitochondria tended to surround the cell's usual two to four nuclei. Rhodamine 123 stained the mitochondria selectively, visualized by fluorescence microscopy. The cell was devoid of cytochromes. Addition of 0.1% cytochrome c to the growth medium increased utilization of glucose by 34% and that of lactate by 17%. Furthermore, it markedly increased the number of mitochondrion-filled cells. At higher concentrations, cytochrome c inhibited the growth of the cells. Despite the presence of large numbers of mitochondria, activities of the mitochondrial enzymes pyruvate dehydrogenase complex, alpha-ketoglutarate dehydrogenase complex, isocitrate dehydrogenase, glutamate dehydrogenase, and cytochrome c oxidase were absent. Thus, the function of the mitochondria in B. hominis remains unknown. Considerable activities of aspartate aminotransferase and alanine aminotransferase were found. Aldolase activity was prominent. Pyruvate decarboxylase was present. Diaphorase and lactate dehydrogenase were detectable but in suspect quantities. Other missing enzymes were gamma glutamyl transpeptidase, alkaline phosphatase (a lysosomal marker), and creatine kinase isoenzymes.
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PMID:Biochemical and ultrastructural study of Blastocystis hominis. 283 9

The marmoset, a small non-human primate, has rarely been used in toxicological studies. A short-term toxicity study was performed on common marmosets (BW = 330 +/- 32 g). Fifteen male marmosets received oral administration of DAB at a dose level of 56 mg/kg/day and 4 control animals received corn oil alone for a period of 15 days. Hematological, biochemical, histopathological and bone marrow examinations were carried out on the 5th, 10th and 15th day of treatment. Body weight decreased continuously and two animals died on day 10. Decreases in RBC, Hb and Ht and increases in MCV and WBC were observed. Uric acid and glucose were increased and AlP and LAP were decreased. Aldolase, GOT and GPT were increased by day 10, and thereafter recovery of aldolase to the control level and decreases of GOT and GPT were observed. Relative organ weights of the liver, kidney, spleen and adrenal were increased. Histologically, C-cell hyperplasia of the thyroid and slight changes of the liver were noted. Marrow total cell counts were not changed, but the G/E ratio was reduced. Thus, macrocytic anemia, an increase of marrow erythroblasts due to anemia and changes of biochemical parameters indicating liver injury were observed in marmosets; these findings were similar to those in rats in the previous experiments.
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PMID:Short-term toxicity study of 4-dimethylaminoazobenzene in marmosets. 310 51

Radioimmunoassays specific for fructose-1, 6-diphosphate aldolase isozymes were developed for the quantification of human aldolase A, B and C. The method is a double-antibody radioimmunoassay using radioiodinated purified aldolase A, B and C as ligand, chicken antibodies to aldolase A, B and C, and rabbit antibodies to chicken IgG. The Iodogen method was used for the iodination of aldolase A, B and C in this study. Aldolase A was predominantly high in concentration in muscle, aldolase B was high in normal adult liver, and aldolase C was high in adult brain. Aldolase A was elevated in hepatoma tissue and hepatoma cell lines, where aldolase B was distinctly low. Normal serum levels for the three isozymes were determined. The aldolase A levels in serum obtained from 41 normal subjects were 170 +/- 39 ng/ml. Serum aldolase A levels were increased in many patients with cancer and muscle diseases, but were not increased in patients with hepatitis or other benign diseases. Serum aldolase B levels obtained from 11 normal subjects were 28.5 +/- 9.2 ng/ml. Serum aldolase B levels were increased in patients with hepatitis and correlated well with serum GPT levels. Serum aldolase C levels obtained from 12 normal subjects were 2.4 +/- 0.7 ng/ml. The determination of aldolase A, B and C by radioimmunoassay may be a valuable tool in biochemical and clinical studies of aldolase isozymes.
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PMID:Subunit-specific radioimmunoassay for aldolase A, B, and C subunits: clinical significance. 632 58

The present study was designed to test if both the intensity and duration of the 45-min Square-Wave Endurance Exercise Test (SWEET) would produce changes in serum enzyme activities. Nine men, four sedentary (S) and five athletes (A), performed VO2 max and SWEET, at their Maximal Intensity of Endurance (MIE45) as defined by maximal heart rate and the impossibility of maintaining MIE 45 + 5% for 45 min. Arterial blood was sampled at rest (R), exercise (Ex) (45th min) and during recovery (15th min) for measurements of levels of Haemoglobin (Hb), Haematocrit (Hct), pH and seven serum enzymes: Creatine kinase (CPK), Hexose-phosphate isomerase (PHI), Aldolase (ALD), Lactate dehydrogenase (LDH), Malate dehydrogenase (MDH), Aspartate amino-transferase (ASAT or GOT), and Alanine aminotransferase (ALAT or GPT). Five enzymes increased significantly during exercise (MIE45), the delta % (Ex - R/R) increases were as follows: PHI (72%), MDH (28%), LDH (21%), CPK (17%), and GOT (13.5%), whilst only a 10% increase was observed for Hct and Hb and there was no significant change in the arterial pH. There was no correlation between the delta % of Hb, Hct, pH, and the results for the enzymes. Thus, it does not seem that haemoconcentration and arterial blood acidosis which occur during exercise are only at the origin of the observed increases in enzymes. A difference between "sedentary" and "athletes" subjects was found at rest and exercise (delta % = A - S/S) for CPK (R = 222%; Ex = 235%), GOT (R = 90%; Ex = 75%) and ALD (R = 99%; Ex = 54%). These results suggest that the MIE45, by measured increases in enzymatic activity, seems to require great muscular effort.
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PMID:Serum enzyme variations in men during an exhaustive "square-wave" endurance exercise test. 653 38

Aiming at investigating biochemical markers of Primary Graft Nonfunction (PNF) in Orthotopic Liver Transplantation (OLT) an experimental work is made on 21 Large-White pigs randomly distributed in three groups of seven, and two additional groups of seven donors each. In Group I the supra and infrahepatic cava, the portal vein and the hepatic artery were clamped. After 30 minutes the caval and portal clamps were released and 30 minutes later the arterial clamp was also removed. In Group II (viable), OLT was performed. The Collins solution was used as preservation fluid, keeping the cold ischemia time under 2 hours. In Group III (Non-Viable), an OLT was carried out 24 hours of cold ischemia with Collins solution. Blood samples are taken in 8 different moments along the procedure to determinate the values of AST, ALT, LDH, FA, Bilirubin, Uric Acid, Cholesterol, Triglycerides, Urea, Creatinine, Glucose, Total Protein, Calcium, Phosphorus, CPK and Aldolase. The last 5 samples were drawn after reperfusion. In the Group III we found, in the samples drawn after reperfusion of the graft, significant increases in 5 of these parameters, AST, ALT LDH, Aldolase and Uric Acid. We consider that these 5 parameters may be of value in the early diagnosis of PNF of the graft, being the AST and ALT the most reliable, with the higher specificity for the same sensitivity.
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PMID:[Biochemical indicators of primary graft dysfunction in experimental orthotopic liver transplantation]. 776 81

We studied the alteration of aldolase isozymes in the serum and tissues of patients with cancer and other diseases using radioimmunoassays specific for aldolase A, B, and C subunits. Aldolase B was predominantly found in adult liver, where aldolase A and C were distinctly low. Aldolase A and B showed almost the same concentration in fetal liver, while in neonatal liver aldolase B protein concentrations were much higher than aldolase A. In contrast, aldolase A was the predominant isozyme found in hepatoma and gastric cancer tissues, whereas aldolase B was distinctly low in hepatoma tissues, and extremely low in gastric cancer tissues. These results suggest that the aldolase A is a more fetal type of liver isozyme than the aldolase B and C, and aldolase B is a more differentiated type of liver isozyme than aldolase A and C. Serum FDP aldolase activities were elevated in half of patients with liver diseases, all patients with muscle diseases and a few patients with cancer. Serum aldolase A levels were elevated in patients with muscle diseases and cancer, but not elevated in patients with liver diseases. In contrast, serum aldolase B levels were elevated in patients with liver disease, but not elevated in patients with muscle diseases and other diseases without liver injury. Serum aldolase B levels showed a trend to decrease in cancer patients with normal GPT levels. Serum aldolase A/B ratios were significantly increased in cancer patients with normal GPT levels, whereas they showed the decreased levels in patients with liver diseases.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Alteration of aldolase isozymes in serum and tissues of patients with cancer and other diseases. 804 42