Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A specific radioimmunoassay was developed for the quantitation of human muscle type aldolase (M-ALD) in human serum. The amount of M-ALD antigen present in 135 sera from normal healthy subjects, noncancer patients and cancer patients was determined. The serum M-ALD value for the 41 normal healthy subjects averaged 171 +/- 39 ng/ml and they had a range from 130 ng/ml to 210 ng/ml. In 33 noncancer hospital patients, excluding patients with muscle diseases, the serum M-ALD values averaged 164 ng/ml and had a range of 125 to 220 ng/ml. In contrast the 61 cancer patients had serum M-ALD values which averaged 586 ng/ml and had a range of 85 to 5800 ng/ml. Eighty two percent of the cancer patients had serum concentrations of M-ALD which were outside of the normal range. The CEA value was determined in the serum of the cancer patients and thirty five percent of the patients had elevated serum concentrations. The measurement of M-ALD values in human serum may be an additional laboratory test in the diagnosis and follow up of the cancer patients.
 ...
PMID:[Clinical study on aldolase isoenzyme--the development of the method of cancer diagnosis with muscle type aldolase (author's transl)]. 23 Oct 1

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.
 ...
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.
 ...
PMID:[Activity of various serum enzymes in calves suffering from nutritionally-induced muscular dystrophy]. 81 73

The author carried out on 35 cats a study on the protein content, potasium and sodium. aldolase, GOT, GPT and LDH of the uterine muscle. The animals were divided into three groups: first-15 nonpregnant cats, second-10 pregnant cats at the first half of pregnancy and third-10 pregnant cats at the second half of pregnancy. He used a piece of uterine muscle from which proteins were extracted by solutions of potasium iodide with various strength. The total protein was determined by the method of Loury, but the sarcoplasmic proteins were examined electrophoretically. Electrolytes were estimated by flame photometer. The enzyme activity was examined by the reagents of "Boehringer". There was an increase of the amount of myosin and of the enzyme active sarcoplasmic protein fraction in the myometrium of pregnant animals. Potasium was increased in the uterine muscle during pregnancy, but sodium decreased. Enxyme activity of ALD, GOT and GPT was the highest in animals from the second group, but that of LDH-in the third group.
 ...
PMID:[Biochemical changes in the myometrium of pregnant cats]. 124 Aug 2

We have studied the effect of T3 administration (50 micrograms/Kg/day) on the phenotype expression of several glucose-metabolizing enzymes (hexokinase, HK, glucose-6-phosphate dehydrogenase, G6P-DH, aldolase, ALD, phosphofructokinase, PFK, lactate dehydrogenase, LDH) in the different myocardial layers of the left ventricle wall. In the control rats, most of these enzyme activities are uniformly distributed across the left ventricle wall, G6P-DH being the only exception. In the rats given T3 for 14 days, the mean levels of PFK, HK and ALD activities increased significantly. With regard to the transmural distribution patterns, that of PFK was unchanged, unlike those of HK and ALD which exhibited their maximum increase in activity in the midmyocardium or in the mid- and subepicardial myocardium. With LDH, a significant increase in activity was found in the subepicardial layers which escaped detection on the whole homogenate. It is concluded that the administration of thyroid hormone has different effects on enzyme phenotype expression of cardiomyocytes in different regions of the cardiac wall.
 ...
PMID:Regional differences in the response of cardiac cells to triiodothyronine administration across the left ventricle free wall of rat heart. 231 6

The age-related changes in the activities of five glucose-metabolizing enzymes (hexokinase, HK; glucose-6-phosphate dehydrogenase, G6P-DH; aldolase, ALD; phosphofructokinase, PFK; and lactate dehydrogenase, LDH) were investigated in the walls of left and right ventricles of rats of various age-groups (1-24 months). Age-related changes were found in the activities of all of the enzymes in both ventricles during growth (with significant decreases between 2 and 6 months of age) and in the levels of PFK and LDH in the left ventricle during ageing (with a significant increase between 12 and 24 months of age). The distribution of the enzyme activities across the wall of both ventricles was quite uniform in young, adult and mature rats (the distribution of G6P-DH activity in the left ventricle wall at 2 months of age was the only notable exception) but became non-uniform in the old rats with regard to G6P-DH, PFK, LDH and probably HK in the left ventricle and G6P-DH and HK in the right ventricle. These data support the hypothesis that alterations connected with ageing do not lead to a generalized decline of cardiac metabolic capacity, and that they are also the result of specific adaptive modifications, perhaps related to alteration in the distribution of the work load and/or of nutrition across the ventricular wall.
 ...
PMID:Changes in the transmural distribution of glucose-metabolizing enzymes across the left and right ventricular wall of rat heart during growth and ageing. 296 12

To investigate whether immunocytochemical localization of muscle-specific aldolase can be used for fiber phenotype determination, we produced specific antibodies against the enzyme and studied its distribution in adult chicken skeletal muscles by indirect immunofluorescence microscopy. Monoclonal antibodies against the myosin heavy chains of fast-twitch (MF-14) and slow-tonic (ALD-58) muscle fibers were also used to correlate aldolase levels with the fiber phenotype. The goat anti-aldolase antibody was found to be specific for the A form of aldolase, as evidenced by sodium dodecyl sulfate gel electrophoresis, immunotitration experiments, and immunoblot analysis. The antibody reacted strongly with the fast-twitch myofibers of normal pectoralis and posterior latissimus dorsi muscles; the phenotype of these muscle fibers was confirmed by a positive immunofluorescent reaction after incubation with MF-14 antibody. By contrast, the slow-tonic myofibers of normal anterior latissimus dorsi, which react positively with ALD-58 antibody, reacted weakly with anti-aldolase antibodies. In denervated chicken muscles, reaction to anti-aldolase antibodies was markedly reduced in fast-twitch fibers, although reaction to MF-14 was not diminished. By contrast, in dystrophic muscle, fast-twitch fibers showed reduced reactivity to anti-aldolase and marked to moderate reduction in MF-14 reactivity. Our results show that: (a) in normal muscles, reactivity to anti-aldolase matches the phenotype obtained by using anti-fast or anti-slow myosin heavy chain antibodies, and therefore can serve to identify mature fibers as fast or slow; and (b) in denervated or dystrophic muscles, the intracellular expressions of aldolase and fast-twitch myosin heavy chains are regulated independently.
 ...
PMID:Immunocytochemical localization of aldolase in normal, denervated, and dystrophic chicken muscles. 327 55

Eight enzymes, e.g. lactate dehydrogenase, malate dehydrogenase, fructose-diphosphate aldolase, sorbitol dehydrogenase, glucose-6-phosphate dehydrogenase, hexokinase, phosphofructokinase and pyruvate kinase were estimated quantitatively in the rat lens from 37 to 1,211 days of age, by spectrophotometric methods. The activity was expressed as mU/g LWW. All enzymes measured showed declining activities, but LDH, ALD, SDH, G-6-PDH, HK and PFK gave a significant decrease during ageing when plotted semi-logarithmically from 37 to 1,211 days. SDH and G-6-PDH showed a statistically significant difference between the enzymes from the male and the female lenses. The female lens always had a lower activity than the male lens. Of all enzymes the specific activity, expressed as mU/l mg protein, was calculated. This specific activity appeared to be rather constant during ageing, except for ALD. In the female lenses, the specific activity of 7 enzymes was lower than in the male lenses. For ALD the specific activity decreased significantly in the male lens from 5.32 at 37 days to 0.88 at 1,211 days. In the female lens this significant decrease was from 4.97 to 0.81.
 ...
PMID:The quantification of eight enzymes from the ageing rat lens, with respect to sex differences and special reference to aldolase. 340 13

A specific radioimmunoassay was developed for the quantification of human muscle type aldolase (M-ALD) in human serum. The method utilized the double antibody radioimmunoassay technique using radioiodinated M-ALD, chicken antibody to M-ALD and rabbit antibody to chicken IgG. The serum M-ALD values of 41 normal healthy subjects ranged from 130 to 210 ng/ml, average 171 +/- 39 ng/ml. In 76 noncancer hospital patients, excluding patients with muscle diseases, the serum M-ALD values ranged from 125 to 220 ng/ml, average 164 +/- 52 ng/ml. In contrast, 129 cancer patients had high serum M-ALD values of 586 +/- 926 ng/ml, ranging from 85 to 5,800 ng/ml. Eighty-six percent of the cancer patients showed serum M-ALD concentrations over the normal range. The measurement of M-ALD values in the serum of patients by radioimmunoassay may be a valuable laboratory test in the diagnosis and follow-up of cancer patients.
 ...
PMID:Diagnosis of cancer by radioimmunoassay of muscle type aldolase. 742 85

Supplement of the deficient neurotransmitters is one of the most effective therapies for neurodegenerative disorders. For the treatment of Parkinson's disease, L-DOPA therapy has been applied to replace dopamine, and droxidopa (L-threo-3,4-dihydroxyphenylserine) therapy to supply noradrenaline (NA). Droxidopa, an artificial amino acid, is decarboxylated by aromatic L-amino acid decarboxylase (AADC) into NA. By application for Parkinson's disease, it alleviated neurological symptoms such as freezing phenomenon, which are refractory to L-DOPA. However, as a precursor of a monoamine, droxidopa was found to be not so effective as L-DOPA; and the clinical efficiency of droxidopa is variable among patients. The metabolic pathway of droxidopa in the brain was examined using human materials. The intraventricular fluid of patients treated with droxidopa, and of control was analyzed by high-performance liquid chromatography with multi-eletrochemical detection (Neurochem). In the intraventricular fluid of the patients treated, free NA concentration increased to be 5.67 +/- 3.40 nM from non-detectable level in the control patients. The patients with higher free NA levels clinically responded better to droxidopa. However, free NA levels varied among patients; and the mechanism of the individual variance should be clarified. In the intraventricular fluid, in addition to NA, a large amount of a metabolite of droxidopa by catechol-O-methyltransferase (COMT), 3-O-methoxy-droxidopa (3OMD), was detected, followed by the metabolites by DOPS-aldolase (DOPS-ALD), protocatechualdehyde and protocatechuic acid. It indicates that considerable parts of administered droxidopa are catabolized by COMT and DOPS-ALD, but not by AADC.(ABSTRACT TRUNCATED AT 250 WORDS)
 ...
PMID:[Study on the metabolism of droxidopa in humans]. 783 60


1 2 Next >>