Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.2.1.20 (alpha-glucosidase)
4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

13C-labeled glycosyl ureides were recently proposed as a new marker of the orocecal transit time: after passing the small bowel the sugar-urea bond is split by bacterial allantoicase. Further degradation results in 13CO2 which can be measured in the exhaled breath. The aim of this study was to detect an eventual allantoicase-like activity in the human gut and to elucidate the metabolism of glycosyl ureides by human intestinal brush border enzymes. Biopsies of 15 duodenal specimen and 6 colon specimen were homogenised and incubated with several disaccharides and their corresponding disaccharide ureides under various experimental conditions. Hydrolysis of the sugar-urea bond could not be observed neither in the small bowel nor in the colon. However, the conjugation between the two sugars was split. In a modified Dahlqvist assay lactase showed the same kinetics with lactose and lactose ureide as substrates whereas maltose showed a significantly 2.6-fold higher affinity to maltase than maltose ureide (P < 0.001). No major difference between these two substrates could be detected when total maltase activity was inhibited by acarbose. In summary, the human gut tissue possesses no allantoicase-like activity. Therefore, glycosyl ureides seem to be appropriate substances to test the orocecal transit time.
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PMID:Metabolism of glycosyl ureides by human intestinal brush border enzymes. 930

Elongation factor Tu (EF-Tu) is involved in the binding and transport of the appropriate codon-specified aminoacyl-tRNA to the aminoacyl site of the ribosome. We report herewith that the Escherichia coli EF-Tu interacts with unfolded and denatured proteins as do molecular chaperones that are involved in protein folding and protein renaturation after stress. EF-Tu promotes the functional folding of citrate synthase and alpha-glucosidase after urea denaturation. It prevents the aggregation of citrate synthase under heat shock conditions, and it forms stable complexes with several unfolded proteins such as reduced carboxymethyl alpha-lactalbumin and unfolded bovine pancreatic trypsin inhibitor. The EF-Tu.GDP complex is much more active than EF-Tu.GTP in stimulating protein renaturation. These chaperone-like functions of EF-Tu occur at concentrations that are at least 20-fold lower than the cellular concentration of this factor. These results suggest that EF-Tu, in addition to its function in translation elongation, might be implicated in protein folding and protection from stress.
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PMID:Chaperone properties of bacterial elongation factor EF-Tu. 956 60

Oral antidiabetics (PAD) are still the most frequent pharmacotherapeutic intervention in NIDDM, characterized by insulin deficiency and in particular by insulin resistance in the liver and peripheral tissues. Depending on the site of action, they are divided into substances retarding carbohydrate breakdown in the small intestine (alpha-glucosidase inhibitors), substances stimulating B-cells of the islets of Langerhans (beta-cytotropic substances) and substances acting in the periphery. The authors discuss PAD, in particular SU and biguanides which have been used for treatment for some years and more recent preparations--acarbose (Glucobay) and miglitol. Attention is paid to perspective preparation which are in the research stage, among them in particular troglitazone which belongs into the group of substances which improve the sensitivity of insulin receptors (insulin sensitizers) which will soon be on the market. As to other possibilities the authors discuss the role of fatty acid oxidation and its inhibitors and new non-sulphonyl urea insulin secretagogues. All these preparations, despite certain limitations, offer exciting therapeutic perspectives. Further research will reveal to what extent this potential can be implemented in practice.
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PMID:[The present and future of treatment with oral antidiabetic agents]. 958 96

We have designed a new method for enzyme immobilization using a fusion protein of yeast alpha-glucosidase containing at its C-terminus a polycationic hexa-arginine fusion peptide. This fusion protein can be directly adsorbed from crude cell extracts on polyanionic matrices in a specific, oriented fashion. Upon noncovalent immobilization by polyionic interactions, the stability of the fusion protein is not affected by pH-, urea-, or thermal-denaturation. Furthermore, the enzymatic properties (specific activity at increasing enzyme concentration, Michaelis constant, or activation energy of the enzymatic reaction) are not influenced by this noncovalent coupling. The operational stability of the coupled enzyme under conditions of continuous substrate conversion is, however, increased significantly compared to the soluble form. Fusion proteins containing polyionic peptide sequences are proposed as versatile tools for the production of immobilized enzyme catalysts.
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PMID:A fusion protein designed for noncovalent immobilization: stability, enzymatic activity, and use in an enzyme reactor. 963 Sep 15

In the treatment of type 2 diabetes (NIDDM) we possess three groups of oral hypoglycaemic drugs: sulfonyl urea derivatives, biguanides (metformin) and alpha-glucosidase (acarbose) inhibitors. Oral treatment of diabetes has a favourable impact on the patients metabolic deviations but it involves also certain dangers and pitfalls. The side-effects of oral antidiabetics can be reduced to a minimum by respecting consequentially contraindications of administration of different preparations, knowledge of their mechanism of action and individual selection of a suitable antidiabetic for every patient.
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PMID:[Pitfalls in treatment with oral antidiabetic agents]. 975 Apr 81

Elongation factor G(EF-G) and initiation factor 2 (IF2) are involved in the translocation of ribosomes on mRNA and in the binding of initiator tRNA to the 30 S ribosomal subunit, respectively. Here we report that the Escherichia coli EF-G and IF2 interact with unfolded and denatured proteins, as do molecular chaperones that are involved in protein folding and protein renaturation after stress. EF-G and IF2 promote the functional folding of citrate synthase and alpha-glucosidase after urea denaturation. They prevent the aggregation of citrate synthase under heat shock conditions, and they form stable complexes with unfolded proteins such as reduced carboxymethyl alpha-lactalbumin. Furthermore, the EF-G and IF2-dependent renaturations of citrate synthase are stimulated by GTP, and the GTPase activity of EF-G and IF2 is stimulated by the permanently unfolded protein, reduced carboxymethyl alpha-lactalbumin. The concentrations at which these chaperone-like functions occur are lower than the cellular concentrations of EF-G and IF2. These results suggest that EF-G and IF2, in addition to their role in translation, might be implicated in protein folding and protection from stress.
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PMID:Chaperone properties of bacterial elongation factor EF-G and initiation factor IF2. 1062 18

The sequence has been determined of 80 888 bp of contiguous subtelomeric DNA, including the isp5 gene, from the right arm of chromosome I of Schizosaccharomyces pombe; 27 open reading frames (ORFs) longer than 100 codons are present, giving a density of one gene per 3.0 kb. Seven of the predicted proteins are members of the major facilitator superfamily (MFS) of transport proteins, including four amino acid permease homologues, bringing this family of amino acid permease sequences to 17 in Sz. pombe, and a phylogenetic analysis is presented. Also encoded is an allantoate permease homologue, a sulphate permease homologue and a probable urea active transporter. Predicted non-membrane proteins include a 1-aminocyclopropane-1-carboxylate deaminase (ACC deaminase), a class III aminotransferase, serine acetyltransferase, protein-L-isoaspartate O-methyltransferase, alpha-glucosidase, alpha-galactosidase, esterase/lipase, oxidoreductase of the short-chain dehydrogenase/reductase (SDR) family, aldehyde dehydrogenase, formamidase, amidase, flavohaemoprotein, a putative translation initiation inhibitor and a protein with similarity to a filamentous fungal conidiation-specific protein. The remaining six ORFs are likely to encode proteins, either because they have sequence similarity with hypothetical proteins or because they are known to be transcribed. Introns are scarce in the sequenced region: only three ORFs contain introns, with only one having multiple introns. The sequenced region also contains a single Tf1 transposon long terminal repeat (LTR). The sequence is derived from cosmid clones c869, c922 and c1039 and has been submitted to the EMBL database under entries SPAC869 (Accession No. AL132779), SPAC922 (AL133522) and SPAC1039 (AL133521).
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PMID:Subtelomeric sequence from the right arm of Schizosaccharomyces pombe chromosome I contains seven permease genes. 1122 45

The eukaryotic cytoskeletal protein tubulin is a heterodimer of two subunits, alpha and beta, and is a building block unit of microtubules. In a previous communication we demonstrated that tubulin possesses chaperone-like activities by preventing the stress-induced aggregation of various proteins (Guha, S., Manna, T. K., Das, K. P., and Bhattacharyya, B. (1998) J. Biol. Chem. 273, 30077-30080). As an extension of this observation, we explored whether tubulin, like other known chaperones, also protected biological activity of proteins against thermal stress or increased the yields of active proteins during refolding from a denatured state. We show here that tubulin not only prevents the thermal aggregation of alcohol dehydrogenase and malic dehydrogenase but also protects them from loss of activity. We also show that tubulin prevents the aggregation of substrates during their refolding from a denatured state and forms a stable complex with denatured substrate. The activity of malic dehydrogenase, alpha-glucosidase, and lactate dehydrogenase during their refolding from urea or guanidium hydrochloride denatured states increased significantly in presence of tubulin compared with that without tubulin. These results suggest that tubulin, in addition to its role in mitosis, cell motility, and other cellular events, might be implicated in protein folding and protection from stress.
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PMID:Chaperone-like activity of tubulin. binding and reactivation of unfolded substrate enzymes. 1150 63

Lysophospholipids are metabolic intermediates in phospholipid turnover, detergent molecules with membrane-modulating effects, and multifunctional cellular growth factors in eukaryotic cells. In bacterial cells, lysophospholipids are mostly found in the form of lysophosphatidylethanolamine. We show that a heat shock from 30 to 42 degrees C increases four-fold the Escherichia coli pool of lysophosphoethanolamine and that lysophospholipids display chaperone-like properties. Lysophosphatidylethanolamine, like molecular chaperones such as DnaK, promotes the functional folding of citrate synthase and alpha-glucosidase after urea denaturation. Like chaperones, lysophophatidylethanolamine, lysophosphatidylcholine, lysophosphatidylinositol and lysophosphatidic acid prevent the aggregation of citrate synthase at 42 degrees C. The renaturation and solubilisation of proteins by lysophospholipids occur at micromolar concentrations of these compounds, close to their critical micellar concentration. Furthermore, lysophosphatidylethanolamine is much more efficient than other detergents tested for the renaturation and solubilisation of citrate synthase. In contrast with lysophospholipids, phosphatidylethanolamine and phosphatidylcholine are not able to promote citrate synthase folding nor to prevent its aggregation at 42 degrees C. The chaperone-like properties of lysophospholipids suggest that, in addition to their known functions, they might affect the structure and function of hydrophilic proteins.
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PMID:Chaperone-like properties of lysophospholipids. 1174 32

Feeding manufactured liquid diets to early-weaned pigs improves growth performance and reduces days to market weight compared with pigs receiving pelleted dry feed. Few alternative dietary ingredients are utilized in manufactured liquid diets other than byproducts of the dairy industry, especially for sources of carbohydrates. This experiment was designed to evaluate the efficacy of starch from partially hydrolyzed corn syrup solids (CSS), at two different levels of hydrolyzation, as a replacement for lactose in manufactured liquid diets. Forty-eight pigs were removed from sows at 1 d of age and randomly assigned to one of three treatments: 1) control with lactose as the carbohydrate source, 2) lactose replaced (gram for gram) with CSS (dextrose equivalent [DE]-20), and 3) lactose replaced with DE-42. In addition, 10 pigs were randomly removed from several litters to provide estimates of initial body composition and small intestinal variables. Twenty-four pigs were removed from the study on d 10 of treatment, and the remaining 24 pigs were removed on d 20 of treatment. Pigs averaged 9,845 +/- 191 g at d 20 of treatment regardless of dietary treatment (P > 0.20). No differences in ADG, ADFI, or feed efficiency were detected between treatment groups from d 0 to 20 (P > 0.19). Whole-body water, protein, lipid, and ash accretion rates were unaffected by dietary treatment from d 0 to 10 or from d 0 to 20 (P > 0.20). The replacement of lactose with CSS did not affect intestinal villi height or width, or crypt depth (P > 0.10). Pigs fed lactose tended to have greater lactase activity on d 10 than pigs fed CSS (P < 0.07). Also, pigs fed lactose tended to have lower oligosaccharidase activity than pigs fed the DE-20 diet on d 20 (P < 0.07). No other differences in lactase, maltase, or long oligosaccharidase specific activity on d 10 or 20 of treatment were detected (P > 0.12). Plasma urea nitrogen concentrations were unaffected by diet on d 10 and 20 of treatment. In addition, dry matter digestibility of the diets averaged approximately 85.6 +/- 0.8% and was unaffected by dietary treatment or day of treatment. These results suggest that partially hydrolyzed CSS can be used as a replacement for lactose in manufactured liquid diets for neonatal pigs.
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PMID:Efficacy of partially hydrolyzed corn syrup solids as a replacement for lactose in manufactured liquid diets for neonatal pigs. 1183 12


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