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)

The effects of feeding 2 protein hydrolysates, one prepared by controlled pepsin and pancreatic protease (including elastase II) hydrolysis of milk proteins (PPPH) and the other a di- and tripeptide bacterial protease hydrolysate of bovine albumin (DTPH), on the growth, nitrogen balance and small intestine adaptation of growing rats were analyzed. Two groups of 3-week-old rats (8 rats/group) were fed the liquid diets ad libitum for 2 weeks. The diets had the same caloric, nitrogen, carbohydrate and lipid contents. The amino acid compositions fulfilled the needs of growing rats. The diet differed in the original proteins, the hydrolysis technique used and the molecular weights of the peptides. Nitrogen intakes were similar. Although there was no difference in weight gain, nitrogen balance was significantly higher in the rats fed the PPPH diet (day 4-day 6:PPPH, 60 +/- 4%, DTPH, 25 +/- 5%; day 12-day 15: PPPH, 58 +/- 3%; DTPH, 30 +/- 5%). The stool nitrogens were identical, suggesting improved nitrogen storage in the rats fed the PPPH diet. Small intestine adaptation showed that the rats on the PPPH diet had significantly more protein (mg) and DNA (microgram) per 10 cm of the jejunum (PPPH, 25.6 +/- 2, 393 +/- 20; DTPH: 15.7 +/- 2, 258 +/- 23) and sucrase-specific activity and per microgram of DNA (PPPH, 133 +/- 5.7, 9.7 +/- 0.5; DTPH, 113 v 5, 7 +/- 1). The N-aminopeptidase-specific activity was the same in both groups.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effects of two protein hydrolysates on growth, nitrogen balance and small intestine adaptation in growing rats. 811 46

We examined the effects of yeast actin NH2-terminal mutations on actomyosin interactions and the function of actin in vivo through measurements of actin-activated ATPase activity, cosedimentation with rabbit muscle myosin subfragment 1 (S-1), in vitro motility, and invertase secretion assays. As reported earlier (Cook, R. K., Blake, W., and Rubenstein, P. A. (1992) J. Biol. Chem. 267, 9430-9436), elimination of NH2-terminal acidic residues from yeast actin results in an increased actin bundling, decreased actin-activated S-1 ATPase, and complete inhibition of actin filament sliding over myosin. Here we show that the addition of 2 new acidic residues to the NH2 terminus of yeast actin increased the Vmax value and the catalytic efficiency of the actin-activated ATPase activity of S-1. However, the binding of actin to S-1 in the presence of ATP and the velocities of actin sliding over myosin in the in vitro motility assays were not affected by this mutation. Thus, the number of actin NH2-terminal negative charges is important for actin activation of myosin S-1 ATPase activity, while only a minimum number of acidic residues is required for actin sliding over myosin in vitro. The number of actin NH2-terminal negative charges therefore appears to determine the efficiency with which the energy from ATP hydrolysis is converted to filament sliding.
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PMID:Enhanced stimulation of myosin subfragment 1 ATPase activity by addition of negatively charged residues to the yeast actin NH2 terminus. 842 14

We have evaluated the fate of misfolded protein domains in the Saccharomyces cerevisiae secretory pathway by fusing mutant forms of the NH2-terminal domain of lambda repressor protein to the secreted protein invertase. The hybrid protein carrying the wild-type repressor domain is mostly secreted to the cell surface, whereas hybrid proteins with amino acid substitutions that cause the repressor domain to be thermodynamically unstable are retained intracellularly. Surprisingly, the retained hybrids are found in the vacuole, where the repressor moiety is degraded by vacuolar proteases. The following observations indicate that receptor-mediated recognition of the mutant repressor domain in the Golgi lumen targets these hybrid fusions to the vacuole. (a) The invertase-repressor fusions, like wild-type invertase, behave as soluble proteins in the ER lumen. (b) Targeting to the vacuole is saturable since overexpression of the hybrids carrying mutant repressor increases the fraction of fusion protein that appears at the cell surface. (c) Finally, deletion of the VPS10 gene, which encodes the transmembrane Golgi receptor responsible for targeting carboxypeptidase Y to the vacuole, causes the mutant hybrids to be diverted to the cell surface. Together these findings suggest that yeast have a salvage pathway for degradation of nonnative luminal proteins by receptor-mediated transport to the vacuole.
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PMID:A pathway for targeting soluble misfolded proteins to the yeast vacuole. 890 38

Two liquid diets containing selected milk proteins (SMP) or its small peptide hydrolysate (SPH) were fed to growing rats for 2 wk and the effects on growth, nitrogen balance, and small intestine adaptation were determined. Residual antigenicity of the SPH diet as measured by immunodot was reduced by 98.8%. Nitrogen intakes were not different. Weight gain was significantly higher in rats fed the SMP diet. In contrast, the absolute nitrogen balance was similar, suggesting that protein storage was identical with the two diets. A better nitrogen digestion-absorption rate with the SPH diet was observed as evidenced by the significantly increased fecal excretion with the SMP diet. Small intestine adaptation showed no difference between the two diets for mucosal weight, protein content/10 cm as well as for sucrase, glucoamylase, and N-aminopeptidase total activity/10 cm or specific activity (mU/mg protein). The DNA content of the mucosa/10 cm was significantly higher suggesting a mucosal hyperplasia in the SPH diet. The data suggest that in rats the SPH diet leads to nitrogen retention and small intestine adaptation similar to that of the SMP diet, despite better body weight gain by the latter.
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PMID:Antigenicity and nutritional value of selected milk proteins and their hydrolysate in growing rats. 897 5

Two analytical methods of sugar determination, namely ion exchange chromatography on an anionic resin coupled with electrochemical detection, and reverse phase chromatography on Nucleosil-NH2 resin equipped with a light scattering detector were tested and compared as regards their rapidity, sensitivity and accuracy with sucrose, fructose, glucose, raffinose, maltose, arabinose, fucose, rhamnose and xylose. Excellent resolution and highly reproducible results were obtained in both cases. Greater sensitivity up to the picomolar range was possible however only with ion exchange chromatography. Reverse phase chromatography was successfully applied to the time course of sucrose hydrolysis under chemical (acid) and enzymatic (invertase) conditions. The hydrolysis was monitored by determining sucrose degradation and the corresponding formation of glucose and fructose.
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PMID:Comparative quantitative analysis of sucrose and related compounds using ion exchange and reverse phase chromatographic methods. 928 24

The synaptojanins represent a subfamily of inositol 5'-phosphatases that contain an NH2-terminal Sac1p homology domain. A nerve terminal-enriched synaptojanin, synaptojanin 1, was previously proposed to participate in the endocytosis of synaptic vesicles and actin function. The genome of Saccharomyces cerevisiae contains three synaptojanin-like genes (SJL1, SJL2 and SJL3), none of which is essential for growth. We report here that a yeast mutant lacking SJL1 and SJL2 (Deltasjl1 Deltasjl2) exhibits a severe defect in receptor-mediated and fluid-phase endocytosis. A less severe endocytic defect is present in a Deltasjl2 Deltasjl3 mutant, while endocytosis is normal in a Deltasjl1 Deltasjl3 mutant. None of the mutants are impaired in invertase secretion. The severity of the endocytic impairment of the sjl double mutants correlates with the severity of actin and polarity defects. Furthermore, the deletion of SJL1 suppresses the temperature-sensitive growth defect of sac6, a mutant in yeast fimbrin, supporting a role for synaptojanin family members in actin function. These findings provide a first direct evidence for a role of synaptojanin family members in endocytosis and provide further evidence for a close link between endocytosis and actin function.
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PMID:Synaptojanin family members are implicated in endocytic membrane traffic in yeast. 978 76

The inhibitory effects of natural and synthetic inhibitors on the intestinal membrane-bound hydrolase, alpha-glucosidase (AGH), were evaluated by using an immobilized cyanogen bromide-activated Sepharose 4B support. Immobilized AGH (iAGH) inhibition study by synthetic inhibitors (acarbose and voglibose) revealed that the magnitude of inhibition differed from that in the free AGH (fAGH) study: IC50 value of acarbose in iAGH-maltase assay system, 340-430 nM; fAGH, 11 nM. iAGH-maltase inhibition by both inhibitors was influenced by blocking reagents with different functional groups (COOH, OH, CH3, and NH2 groups). On the other hand, significant iAGH-sucrase inhibitory activity was observed only when using the negatively charged support induced by 0.1 M beta-alanine. The Km values obtained in the iAGH assay system were similar to those from the fAGH method. With natural inhibitors, the iAGH-sucrase inhibitory activity of D-Xylose, with in vivo glucose suppression, increased twice compared to that in fAGH. Green tea extract gave almost the same inhibition for both AGH assay systems.
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PMID:Evaluation of alpha-glucosidase inhibition by using an immobilized assay system. 1099 9

The digestion and nutritive value of defatted grape seed meal (DGSM) was investigated. A basal diet was formulated to meet requirements of growing rabbits. Another diet was formulated by substituting 15.2% of the basal diet with DGSM. Two hundred eight weaned 30-d-old rabbits were fed these diets, and fattening performance was recorded. Eighty animals were used to study the effect of DGSM inclusion on cecal fermentation traits and intestinal disaccharidase activity at two ages (5 and 35 d after weaning). Fecal apparent digestibility of nutrients was measured in 18 rabbits. A third diet was formulated to contain DGSM (61.3%) as the sole source of fiber and a supplement consisting of wheat flour, casein, lard, and a mixture of vitamins and minerals to avoid nutrient imbalances. This semipurified diet was used to determine cecal digestion traits, disaccharidase activity in the small intestine, fecal apparent digestibility of nutrients, and rate of passage in 70-d-old rabbits. Digestible energy and NDF and CP digestibilities of DGSM calculated by difference were 5.51 +/- 0.89 MJ/kg DM, 24.5 +/- 5.76%, and 46.8 +/- 14.9%, respectively. Inclusion of 15% of DGSM in the basal diet increased ADFI in finishing rabbits (from 9 to 15%; P < 0.05), so that DE intake increased although dietary DE concentration decreased. As a consequence, ADG increased by 3.3% in the whole fattening period (P = 0.046). The increase in ADFI was parallel to an 8% decrease in the weight of cecal contents (P = 0.059), and it was in agreement with the relatively short cecal mean retention time of DGSM (7.61 h) in the semipurified diet. Inclusion of 15% of DGSM in the basal diet did not affect (P > or = 0.20) mortality (10.1%) or cecal concentrations of VFA, NH3 N, or cecal pH either at 5 d (71.9 mM, 17.7 mM, and 5.75, respectively) or at 35 d after weaning (74.6 mM, 10.1 mM, and 5.66, respectively) but improved the sucrase activity in the ileum by 36% (P = 0.031). Digestibility of NDF of DGSM in the semipurified diet was 8.57%, which agrees with the low acidity and weight of cecal contents of animals fed this diet (6.26 and 3.63% BW, respectively). From these results, we conclude that DGSM has a relatively high DE concentration and its inclusion at moderate levels (15%) in the diet exerts a positive effect on ADFI, DE intake, and ADG with no impairment of cecal fermentation and mortality.
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PMID:Effect of inclusion of defatted grape seed meal in the diet on digestion and performance of growing rabbits. 1183 33

Knowing that human blood monocyte-derived dendritic cells express cell-surface mannose-specific lectins, we prepared various mannoses containing glycoconjugates with the aim of developing highly specific synthetic carriers of oligonucleotides and genes. Conjugates were prepared from oligosaccharides obtained by hydrazinolysis of Saccharomyces cerevisiae invertase glycopeptides. The reducing saccharides were converted into glycosynthons, i.e., into glyco-amino acids. Fluorescein derivatives were obtained by coupling the free carboxyl group of oligosaccharyl-pyroglutamate to the alpha-amino group of epsilon-fluoresceinyl-thiocarbamyl lysine methyl ester. It has been shown by others that glycosylated linear oligolysines containing up to six alpha-D-mannopyranosylphenylthiocarbamyl units have a high affinity for the human mannose receptor. In order to obtain fully biodegradable clusters and to improve both the specificity and the selectivity, disaccharides transformed into glycosynthons were coupled to pentalysine carriers (Lys5-Ala-Cys-NH2). Glycosylated pentalysyl cysteine conjugates were made fluorescent upon substitution of the cysteine thiol group with fluorescein iodoacetamide. As shown by flow cytofluorimetry, both the dimannoside clusters and yeast oligomannosides were very efficiently taken up by DC, conversely lactoside clusters were not.
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PMID:Uptake of dimannoside clusters and oligomannosides by human dendritic cells. 1216 31

Callus cultures derived from pith tissue of Nicotiana tabacum were grown on two media either under continuous illumination or in complete darkness. The first medium limited greening ability of callus grown in the light (3 milligrams per liter naphthalene acetic acid, 0.3 milligram per liter 2-isopentenylaminopurine, Murashige and Skoog salts, and 2% sucrose). The second medium encouraged chlorophyll synthesis (greening) though not shoot formation (0.3 milligram per liter naphthalene acetic acid; 0.3 milligrans per liter 2-isopentylaminopurine). To measure intracellular concentrations, calli were grown for 15 days on these standard media containing [U-(14)C]sucrose. The dry weight proportions of the calli (as a fraction of fresh weight) and many metabolite concentrations nearly doubled in light-grown cells compared to dark-grown cells and increased 30 to 40% on low-auxin media relative to high-auxin media. Glutamine concentrations (from 4 to 26 millimolar) were very high, probably due to the NH(3) content of the media. Proline concentrations were 20-fold higher in calli grown on low-auxin media in the light (green cells), possibly a stress response to high osmotic potentials in these cells. To analyze sucrose metabolism, callus cells were allowed to take up 0.2% (weight per volume) [U-(14)C]sucrose for up to 90 minutes. In callus tissues and in pith sections from stems of tobacco plants, sucrose was primarily metabolized through invertase activity, producing equal amounts of labeled glucose and fructose. Respiration of (14)CO(2) followed the labeling patterns of tricarboxylic acid cycle intermediates. Photorespiration activity was low.
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PMID:Intracellular concentrations and metabolism of carbon compounds in tobacco callus cultures: effects of light and auxin. 1666 13


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