Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Statistical analysis of variance was applied to data from determinations of 14 plasma constituents in 25 rats in order to evaluate the analytical, experimental and biological (inter-and intraindividual) component of variance. Blood was taken seven times in intervals of 8-10 days, the last one by catheter technique and the other by heart puncture. The analytical portion of variance was determined by the concurrent analysis of a pool plasma standard. The experimental component of variance was evaluated by the comparison of the variation of the catheter values with that of the pooled data from heart puncture. The coefficient of variation for the latter may be grouped into three categories: less than 10% for protein, Na+, K+, Ca2+; 10-20% for urea, phosphate and the enzymes as alanine aminotransferase, choline esterase, alkaline phosphatase and leucine arylamidase and 20-65% for the other enzymes lactate dehydrogenase, malate dehydrogenase, aspartate aminotransferase and creatine kinase. The results from the samples taken by catheter technique generally revealed the lower values for the mean as well as for the variance. It became evident that the procedure of heart puncture is afflicted with the most aggravating interference factors, thus accounting for most of the experimental component of variance. The observed differences between the single blood drawings, the non-Gaussian distribution for several constituents, and the interactions between the components of variance do not always fit for the statistical concept of additivity of the single components.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Biological, analytical and experimental components of variance in a long-term study of plasma constituents in rat. 660 70

Isozyme patterns of 23 different enzymes were compared in normal, benign, and malignant breast tissues; in MCF-7 cells; and in organoids of normal human breast tissue. Benign lesions generally showed isozyme patterns similar to those of normal tissues. Lactate dehydrogenase isozyme 5 was significantly increased in malignant tumors; MCF-7 cells had only lactate dehydrogenase (L-lactate:NAD oxidoreductase; EC 1.1.1.27). The mitochondrial form of malate dehydrogenase was also significantly increased in human malignant tumors; this was especially evident when comparing tumor and apparently uninvolved breast tissue from the same patient. The K4 isozyme of pyruvate kinase was the major form in most malignant breast tumors, but in only 41% of normal tissues, 30% of fibrocystic disease specimens, and 46% of fibroadenomas. A more anodal band of pyruvate kinase, probably a K3M or K3Kpm hybrid, predominated in most normal and benign tissues, but in only 63% of primary and 56% of secondary tumors. All specimens had predominantly creatine kinase BB, aldolase A4, and hexokinase I. Traces of aldolase A3C and of hexokinase II were observed in some tumors. None of the tumors had the Regan variant of alkaline phosphatase. The isozymes of lactate and malate dehydrogenases and of pyruvate kinase appear to be the most promising as putative tumor markers.
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PMID:Isozyme patterns of normal, benign, and malignant human breast tissues. 664 May 38

The isozyme patterns and activities of six enzymes were determined in surgical biopsy samples of lung tumors and non-neoplastic pulmonary areas. Fetal lungs were also examined. No tissue differences were found in the isozyme pattern of hexokinase or alkaline phosphatase; small differences in pyruvate kinase isozyme proportions were observed. The tumors exhibited significant deviations with respect to the lactate dehydrogenase (LDH) and malate dehydrogenase (MDH) isozyme patterns. Despite the diversity of cell types, the proportions of the M-subunit of LDH in each tumor and that of the mitochondrial isozyme of MDH in all but one tumor were higher than in control samples from the same lung. In contrast, the normal fetal lung showed a higher LDH-H proportion than did adult lung and a mature MDH isozyme pattern. The alpha-glycerophosphate dehydrogenase and adenylate kinase activities of the tumors were about one-tenth and one-fourth, respectively, of those of nonneoplastic adult lung. These lower activities (evident also in normal fetal lung) were accompanied by 3- to 5-fold increases in the LDH, MDH, pyruvate kinase, and hexokinase activities of the tumors; fetal lungs had lesser increases (2- to 3-fold) for the first 3 enzymes. The common features of tumors with different cell types and histological grade identified here point to several enzymes the quantitation or isozyme analysis of which may be of practical use in distinguishing cancerous from nonneoplastic human lung samples. A combination of different indicators, such as opposite changes in LDH and alpha-glycerophosphate dehydrogenase activity, coupled with elevated proportions of LDH-M, may be used to diagnose neoplasia most reliably.
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PMID:Enzyme activities and isozyme patterns in human lung tumors. 669 92

Rectal biopsy specimens from control subjects, patients with either active or quiescent ulcerative colitis, and patients with Crohn's colitis were examined histologically and assayed for marker enzymes associated with tissue organelles. They were catalase (peroxisome); neutral alpha-glucosidase (endoplasmic reticulum); alkaline phosphatase (plasma membrane); malate dehydrogenase (mitochondria); lactate dehydrogenase (cytosol). There was no significant change in these enzyme activities in patient samples compared with controls. Activities of three acid hydrolases (lysosomal enzymes), beta-glucuronidase, acid phosphatase, and N-acetyl-beta-glucosaminidase, were also assayed in the biopsy samples. Decreased activities of all three enzymes were noted in ulcerative colitis, particularly in active disease. Normal values were obtained in Crohn's colitis. Measurement of lysosomal integrity by assays of latent N-acetyl-beta-glucosaminidase activity revealed similar results in control and colitic subjects. It is suggested that the lysosomal changes reflect a specific tissue release of enzyme and may be implicated in the pathogenesis of the tissue damage.
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PMID:Organelle pathology in ulcerative and Crohn's colitis with special reference to the lysosomal alterations. 671 88

The circular dichroism bands of (+) gossypol in the spectral region 300-400 nm have been shown to be sensitive to interactions with proteins. Using CD spectroscopy, gossypol has been shown to interact with lactate dehydrogenase, malate dehydrogenase, alkaline phosphatase, lysozyme, protamine and poly-L-lysine. Binding to proteins generally results in a pronounced red shift of the long wavelength CD band (approximately 380-430 nm) accompanied by a reduction in ellipticity. The changes in spectral parameters of the 1Lb binaphthyl transition may reflect a distortion from a nearly perpendicular gossypol conformation, on binding to proteins.
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PMID:A circular dichroism study of (+) gossypol binding to proteins. 674 22

The article deals with the results of histochemical study of some redox and proteolytic enzymes (SDH, MDH, NAD-diaphorase, LDH, and acid and alkaline phosphatase) in experiments on animals in various periods after infliction of a craniocerebral injury and on autopsy material, i.e. the brain of patients who had died from severe craniocerebral injury incompatible with life. It is shown that the activity of all enzymes decreases (SDH, MDH, NAD-diaphorase, and alkaline phosphatase) or increases (LDH, acid phosphatase) in various periods after the injury. The results were compared with the findings of morphological examination of the same brain areas performed by means of neurohistological methods.
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PMID:[Redox and proteolytic enzymes in brain tissue after a concussion]. 689 60

For the purpose of describing early chondrogenic metabolic and structural events, measurements were made of oxidative and other enzymatic activities at various stages in the morphologic development of chondrocytes over a period of 18 to 20 days in continuous cell culture. Comparisons were also made between cells grown in 20% O2 and in 35% O2. These cultures exhibited rapid confluence (within 24 hours), early development of cartilaginous nodules by Day 2 to 3 and metachromatic staining of the chondrocyte matrix by Day 3 to 4. Under 35% O2, cell sheets were thicker and there was increased pleomorphism of chondrocyte and fibroblast cell types, with a relative increase of fibroblast components and reduction in chondroblasts and chondrocyte aggregates. Using the von Kossa staining procedure, calcium salt deposition was observed by Day 9. There was no apparent difference in mineralization of cultures grown under the low and high O2 tensions. Under normoxic conditions cytochrome oxidase and malate dehydrogenase (MDH) activities increased rapidly for the first three to four days and then remained essentially constant. Lactate dehydrogenase (LDH) activity increased continuously over the life of the culture. Acid phosphatase increased rapidly until about Day 13 after which it remained constant, whereas alkaline phosphatase showed a bimodal activity profile. Under hyperoxic conditions, cytochrome oxidase, MDH and alkaline phosphatase activity were significantly inhibited. LDH and acid phosphatase activities were markedly inhibited initially but with time showed a degree of recovery.
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PMID:Development of chick limb bud chondrocytes in cell culture: morphologic and oxidative metabolic observations. 701 57

The activity of serum enzymes, such as, creatine kinase (CK), pyruvate kinase (PK), aldolase (ALD), lactate dehydrogenase (LDH), sorbitol dehydrogenase (SbDH), malate dehydrogenase (MDH), glutamate-aspartate aminotransferase (AST), glutamate-alanine aminotransferase (ALT), myokinase (MK), glucosephosphate isomerase (GPI), alkaline phosphatase (AlkP), pseudocholinesterase (PsCHE) isocitrate dehydrogenase and gamma-glutamyltranspeptidase (gamma-GTP), was determined in 256 patients with progressing myodystrophy (PMD) (Duchenne's form in 125, Becker's form in 14, pelvicohumeral form in 36, humeroscapulofacial form in 19, ocular form in 10, other rare forms in 34, and nonidentified forms in 13 patients). In the control group (64 men, 56 women and 50 children), the activity of the enzymes was found to depend on the patients' sex and age. With regard to both parameters, i. e. the degree of the enzyme activity rise and the frequency of the pathological values the most informative were CK, then PK and ALD, and then all the other enzymes. Of all the PMD forms the enzymatic activity appeared to be the highest in patients with the pseudohypertrophic malignant form. By determining the activity of five enzymes (CK, ALD, LDH, AST and ALT) and taking into consideration the patient's age, the onset and the duration of the disease one can distinguish between sick and healthy subjects, as well as between various forms of PMD.
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PMID:[Serum enzyme dynamics in progressive muscular dystrophies]. 703 17

Portions of jejunal biopsies from control subjects and from patients with coeliac disease were cultured for 24 hours using an in vitro organ culture technique. Alkaline phosphatase activity was measured in the tissue and medium before and after culture; enzyme activities were expressed per microgram tissue DNA. The increase in enzyme activity during the culture period was taken to represent net enzyme synthesis. Alkaline phosphatase synthesis by mucosa from patients with untreated gluten-sensitive coeliac disease and by mucosa from patients with non-responsive coeliac disease was significantly less than that by normal mucosa. Alkaline phosphatase synthesis by mucosa from patients with treated gluten-sensitive coeliac disease was greater than that by untreated coeliac mucosa but was less than normal mucosa. Sequential studies of alkaline phosphatase synthesis by jejunal mucosa from seven patients with coeliac disease, before and after successful treatment by gluten withdrawal, showed an increase in synthesis in all patients. Study, by analytical subcellular fractionation with sucrose density gradient centrifugation, of the properties of the organelles of cultured control tissue showed good preservation of their integrity. A striking finding, however, was the decrease in malate dehydrogenase with a corresponding marked increase in lactate dehydrogenase. This would be expected to be followed by a shift from aerobic to anaerobic metabolism. Analytical subcellular fractionation of cultured mucosa from patients with coeliac disease gave similar conclusions. There was, however, a marked improvement of the brush border abnormalities, characteristic of coeliac disease, during culture with increased enzyme activities and membrane equilibrium density in the sucrose gradients.
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PMID:Alkaline phosphatase synthesis and properties of subcellular organelles during in vitro culture of jejunal biopsies from control subjects and patients with coeliac disease. 706 34

A high dose of niridazole administered intraperitoneally (i.p.) to male rats over a period of 9 weeks induced alterations in the concentrations and activities of some important testicular constituents and enzymes, respectively. The concentrations of total and free cholesterol were higher than those of control animals but the concentration of esterified cholesterol was significantly lower than that of the control rats. Zinc concentration in the testis and prostate gland of niridazole-treated animals was significantly lower than in the control animals. Decreases in the activities of the following enzymes occurred in the testes of niridazole-treated rats: lactate and sorbitol dehydrogenases, aspartate and alanine aminotransferases and alkaline phosphatase. By contrast, there were increases in the activities of testicular malate dehydrogenase and prostate acid phosphatase of rats given niridazole.
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PMID:Niridazole-induced biochemical changes in the rat testis. 716 74


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