Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.26 (invertase)
 4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Gastric and intestinal phenotypic expression in 37 surgically obtained primary signet ring cell carcinomas, five of their metastases to lymph nodes, and three signet ring cell carcinomas transplanted into nude mice were determined by biochemical, mucin, histochemical, and ultrastructural studies. Crude extracts of cancer tissues were used for measurements of pepsinogen isozymes, sucrase, aminopeptidase (microsomal), and alkaline phosphatase. Histochemical staining of mucin by paradoxical concanavalin A, the galactose oxidase-Schiff sequence and sialidase-galactose oxidase-Schiff, and the periodate-borohydride technique/potassium hydroxide/periodic acid-Schiff procedure was performed. The procedures allowed clear definition of pyloric gland, surface mucous, small and large intestinal goblet, and intestinal absorptive cell types. Of 40 specimens examined, 19 consisted entirely of gastric-type cells, and three entirely of intestinal-type cells. The others consisted of mixtures of gastric and intestinal-type cells. The observed high incidence of intestinal-type cells in signet ring cell carcinomas suggested that intestinal-type cells develop independently from intestinal metaplasia within signet ring cell carcinomas (diffuse-type gastric cancers), which probably originate from nonmetaplastic gastric mucosa.
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PMID:Gastric and intestinal phenotypic expressions of human signet ring cell carcinomas revealed by their biochemistry, mucin histochemistry, and ultrastructure. 301

There is a reported association between administration of prenatal glucocorticoids and a decreased incidence of necrotizing enterocolitis in human infants. In rats, the degree of ischemic bowel disease correlates negatively with intestinal diamine oxidase (E.C. 1.4.3.6) activity. Since the administration of hydrocortisone, thyroxine, or phenobarbital to newborn rat pups affects the development of intestinal enzymes, we were interested in knowing whether hydrocortisone, thyroxine, or phenobarbital specifically affect intestinal diamine oxidase activity. We injected rat pups with hydrocortisone sodium succinate, 1-thyroxine pentahydrate, sodium salt, sodium phenobarbital, or the control solution on days 4, 6, 8, or 10 of life (phenobarbital, days 3, 5, 7, or 9). Pups were injected 3 days consecutively (phenobarbital, 4 days), and all were sacrificed on days 7, 9, 11, and 13. Intestinal diamine oxidase and intestinal invertase (E.C. 3.2.1.26) activities were measured. Invertase was used as a control enzyme because it is known to be induced by glucocorticoid hormones. We found that the hydrocortisone-injected pups had 10-fold higher specific activity of invertase than the saline-injected animals. Diamine oxidase activity was significantly higher in the group receiving hydrocortisone and sacrificed on days 7, 9, and 11. Enzyme activity in both the hydrocortisone-injected and saline-injected groups was equal on day 13, as was enzyme activity on all days in the thyroxine-injected and sodium hydroxide-injected groups, and the phenobarbital-injected and the saline-injected groups. Our results suggest that diamine oxidase activity may be induced by hydrocortisone, but is not affected by thyroxine or phenobarbital.
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PMID:The effect of hydrocortisone, thyroxine, and phenobarbital on diamine oxidase activity in newborn rat intestine. 310 23

1. A study was made of the composition and structure of walls isolated from yeast grown in continuous culture at different rates, under three conditions of glucose limitation in which the concentrations of glucose and ammonium sulphate in the medium and the oxygen-transfer rate in the culture were varied, and one condition of NH(4) (+) limitation. 2. The contents of total glucan and total mannan in the walls were relatively little affected by the growth rate under any of the four sets of conditions. The phosphorus and protein contents of walls from yeast grown under each of the four conditions increased as the growth rate was decreased. Walls from yeast grown under NH(4) (+) limitation contained only half as much protein as walls from cells grown under glucose limitation. The proportion of lipid was greatest in walls from yeast grown under NH(4) (+) limitation. 3. A procedure was devised for fractionating isolated walls, based on the ease with which the glucan and mannan were extracted with water and with hot and cold 6% (w/v) potassium hydroxide solution. The percentage of glucan, mannan, protein and phosphorus in each of the fractions was affected by the rate of growth and by the nature of the substrate limitation. 4. The beta-fructofuranosidase activities of yeast grown under glucose limitation increased as the growth rate was lowered, but decreased at very low growth rates. The effects at low growth rates were probably due to repression of enzyme synthesis by residual glucose in the culture filtrate. The beta-fructofuranosidase activities of yeast grown under NH(4) (+) limitation were much lower than those from yeast grown under any of the conditions of glucose limitation. 5. Yeast cells grown at any of the rates under NH(4) (+) limitation were longer and thinner than those grown at the same rate under any of the conditions of glucose limitation. Mean cell volumes were dependent on growth rate but not on the nature of the substrate limitation. 6. Electron micrographs of thin sections of isolated walls showed that cells grown under NH(4) (+) limitation had a more porous structure than those from cells grown under any of the conditions of glucose limitation.
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PMID:Effect of growth rate and substrate limitation on the composition and structure of the cell wall of Saccharomyces cerevisiae. 605 21

The determination of the invertase activity of intact yeast cells presents a critical point, that is, the blockage of the enzyme action at a given moment. In this paper seven blockage methods were compared: the addition of 0.010 M sodium hydroxide solution, addition of 0.010 M sodium carbonate solution, addition of 0.010 M sodium carbonate solution followed by centrifugation (9750g; 10 min), immersion of the reacting mixture in a boiling water bath, immersion of the mixture in a -15 degrees C bath, filtration through a Millipore membrane, and addition of the first Somogyi's reagent followed by immersion in a boiling water bath. Only the last two methods lead to a rapid and effective blockage of the invertase activity.
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PMID:Measurement of invertase activity of cells of Saccharomyces cerevisiae. 634 48

Sugar beet and sugar cane molasses have been shown to be suitable starting materials for producing de-icer preparations. The sucrose in the molasses is hydrolyzed to glucose and fructose by invertase. The reducing sugars are then degraded by NaOH, the alkali being neutralized by the sugar acids produced, resulting in an increase of the ionic strength and consequently depression of the freezing point of the resulting solution. For the preparation of de-icers, the desired freezing point depression to a temperature of less than about -20 degrees C can be achieved by adjusting the amount and concentration of the alkali metal hydroxide used. The resulting products are biodegradable and eliminate the corrosive effects associated with the use of conventional chloride salts. Degradation of invert sugar by NaOH has been achieved without an external heat source. The reaction products showed the same freezing point depression as seen in the degradation products from pure glucose.
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PMID:Alkaline degradation of invert sugar from molasses. 1722 51

Hydroxyl radical footprinting (HRF) is a nonspecific protein footprinting method that has been increasingly used in recent years to analyze protein structure. The method oxidatively modifies solvent accessible sites in proteins, which changes upon alterations in the protein, such as ligand binding or a change in conformation. For HRF to provide accurate structural information, the method must probe the native structure of proteins. This requires careful experimental controls since an abundance of oxidative modifications can induce protein unfolding. Fast photochemical oxidation of proteins (FPOP) is a HRF method that generates hydroxyl radicals via photo-dissociation of hydrogen peroxide using an excimer laser. The addition of a radical scavenger to the FPOP reaction reduces the lifetime of the radical, limiting the levels of protein oxidation. A direct assay is needed to ensure FPOP is probing the native conformation of the protein. Here, we report using enzymatic activity as a direct assay to validate that FPOP is probing the native structure of proteins. By measuring the catalytic activity of lysozyme and invertase after FPOP modification, we demonstrate that FPOP does not induce protein unfolding.
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PMID:Modifications generated by fast photochemical oxidation of proteins reflect the native conformations of proteins. 2957 96