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)

A pleiotropic mutation in Neurospora (exo-1), which confers derepression of alpha-amylase, glucoamylase, beta-fructofuranosidase, and trehalase, appears to also affect the composition of the cell wall. Segregants resulting from the backcross of exo-1 to the wild-type strain from which it derived are altered in the ratio of galactosamine to glucosamine in hydrolysates of isolated cell walls. Conidial cell walls exhibit a marked decrease in the amount of galactosamine in both exo-1 and exo-1(+) strains. Increased levels (approximately sevenfold) of amylase are found in conidia of exo-1, as compared with those of exo-1(+).
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PMID:Cell wall alterations associated with the hyperproduction of extracellular enzymes in Neurospora crassa. 426 2

Trevithick, John R. (University of Wisconsin Medical School, Madison), Robert L. Metzenberg and Donald F. Costello. Genetic alteration of pore size and other properties of the Neurospora cell wall. J. Bacteriol. 92:1016-1020. 1966.-Several properties of the cell walls of wild type and the osmotic mutant of Neurospora crassa have been examined. The peameability of the isolated cell walls to polyethylene glycol and dextran polymers of different molecular weights was investigated by the volume of distribution technique. The exclusion thresholds were evaluated by a statistical treatment. The molecular weights corresponding to these thresholds for wild type and osmotic were approximately 4,750 and 18,500, respectively; these values are significantly different. The cell walls of osmotic appeared to be thinner, more easily broken, and more easily compressed to ribbonlike shapes, whereas those of wild type were tubular and strong. Chemical analysis showed that osmotic walls had roughly a 30-fold higher galactosamine-glucosamine ratio than did wild type. It is proposed that the osmotic mutant has a cell wall with abnormally large pores, and that this may account for the increased rate of egress of invertase and the decreased fractionation of light from heavy invertase in this strain.
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PMID:Genetic alteration of pore size and other properties of the Neurospora cell wall. 592 38

The activities of lactase, sucrase, maltase and gamma-glutamyl transferase (gamma-GT) were determined in homogenates of rat jejunal mucosa 24 h after acute administrations of D-galactosamine (GALN) (1.855 mmol/kg; i.p. injection) and alpha-naphthyl-isocyanate (ANIT) (0.540 mmol/kg; given by gastric tube). The animals were fasted either 24 h or 72 h prior to sacrifice. In rats fasted only 24 h, GALN treatment resulted in a pronounced decrease in lactase and in a moderate elevation of sucrase and maltase. ANIT clearly reduced lactase and, to a lesser extent, sucrase, while it increased maltase. Seventy-two hour fasting has a modifying role. All disaccharidase activities tended to decrease, except for maltase in the ANIT treated group, where an increase was recorded. gamma-GT showed no significant changes after either GALN or ANIT treatment in rats fasted 24 h. However, the 72-hour food deprivation diminished it in ANIT intoxication. It is obvious that the intestinal enzymes are influenced by the hepatic damage produced by GALN and ANIT.
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PMID:Influence of D-galactosamine and alpha-naphthylisothiocyanate on the activities of some intestinal enzymes. 615 Aug 89

Laminin was purified to homogeneity from the extracellular matrix and soluble fraction of teratocarcinoma OTT6050 and also partially purified from the ascitic fluid of the mice carrying the teratocarcinoma. These laminin preparations were found to agglutinate trypsinized, glutaraldehyde-fixed rabbit erythrocytes. The hemagglutinating activity was inhibited by porcine gastric mucin, which invertase and mannan were not inhibitory. Heparin and heparan sulfate also inhibited the hemagglutination. Simple saccharides such as D-galactose, N-acetyl D-glucosamine, and N-acetyl D-galactosamine were not inhibitory, but D-glucosamine and D-galactosamine were. The hemagglutinating activity required Ca2+ and was dependent upon temperature. These results raised the possibility that laminin functions also in cell-cell interactions such as cell-cell adhesion. In addition, we report that laminin synthesized by the teratocarcinoma did not carry the large carbohydrate chain characteristic of early embryonic cells.
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PMID:Basement membrane glycoprotein laminin is an agglutinin. 663 Jan 69