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At least 19 recordsLinked to original sources

PubMed1975

Isolation of amylopectin granules and identification of amylopectin phosphorylase in the oocysts of Eimeria tenella.

Amylopectin granules were purified from Eimeria tenella oocysts following digestion with sodium dodecyl sulfate and pronase. The oval granules had a uniform size of 0.5 X 0.7 mum, and consisted of only glucose polymers. alpha-Amylase treatment yielded 235 nmoles of maltose from the granules from 10(6) unsporulated oocysts and 93 nmoles maltose from those from 10(6) sporulated oocysts. Amylopectin phosphorylase activity was detected in the cytoplasm of unsporulated oocysts of E. tenella. It had a specific activity of 13 U/mg protein in crude extracts, and a pH optimum of 6.0. The Km values determined were 9.1 mM for glucose-1-phosphate and 5.6 mM for glucose end groups in potato amylopectin. Enzyme activity declined at a linear rate during sporulation, sporulated oocysts containing less than 8% of the activity of unsporulated oocysts. No amylase-type activity was found in the parasite.

Amylopectin↗

PubMed1991

Starch flavor: apparent discrimination between amylopectin and amylose by rats.

Rats given a choice between dilute suspensions of corn amylopectin and corn amylose generally preferred amylopectin. The preference threshold for amylopectin was lower than the preference threshold for amylose (0.1% and 0.5%, respectively). Two sources of evidence indicate that the difference in preference for these two types of starch is due to an off-taste component in corn amylose rather than to an ability to discriminate between amylopectin and amylose per se: 1) rats given a choice of purified amylopectin and amylose from potato did not show a significant preference, and 2) aqueous extracts of amylose reduce preference for water and amylopectin, respectively. Extensive washing of corn amylose with ammonia-methanol, water and methanol did not completely remove the off-taste of corn amylose. Despite the difference in off-taste, rats trained to avoid amylopectin also avoided amylose. It is proposed that starch has two flavor components: a component due to starch itself that induces preference, and a component due to impurities that reduces preference.

Amylopectin↗

PubMed1975

Studies on the binding of amylopectin sulfate with gastric mucin.

Amylopectin sulfate, a sulfated polysaccharide that has an antipeptic property, was examined for its ability to bind gastric mucins. After chemically cross-linking the amylopectin sulfate into an insoluble gel, its binding with mucins isolated from antral and fundic mucosa of canine stomachs was studied with chromatography. A component present in both mucin fractions bound to the amylopectin sulfate gel below pH 4.5. This binding was reversible, and the complex dissociated above pH 5. Similar binding properties were found with soluble amylopectin sulfate. The component of the mucine which bound to amylopectin sulfate differed from the one which did not bind in its electrophoretic mobility and in its higher proportion of basic amino acids and a lower hexosamine, serine, and threonine content. This study suggests that amylopectin sulfate may bind to gastric mucins only under conditions of low pH.

Amino Acids↗

PubMed1985

Induction of colorectal adenocarcinoma in rats by amylopectin sulfate.

The carcinogenicity of orally administered amylopectin sulfate was studied in F344 rats. Amylopectin sulfate induced adenomas and adenocarcinomas in the rat colorectum. The incidences of tumor induction in groups that were given a 5% diet of amylopectin sulfate for 3, 6 and 9 months were 2 out of 20 rats (10%), 9 out of 20 rats (45%) and 12 out of 20 rats (60%), respectively. Squamous metaplasia of the colorectum persisted in all rats and progressed irreversibly. Amylopectin sulfate was deposited in the colorectal lamina propria, submucosa and regional lymph nodes. Amylopectin sulfate induced a lesion similar to that produced by degraded carrageenan in the rat colorectum.

Adenocarcinoma↗

PubMed1985

Rapid analysis of starch, amylose and amylopectin by high-performance size-exclusion chromatography.

Starch components, amylose and amylopectin, were analyzed by high-performance size-exclusion chromatography. These two-components were separated using a two-column system (E-Linear and E-1000) and dimethyl sulphoxide as the mobile phase. The void volume (V0 = 2.22 ml) was measured using tobacco mosaic virus. Column calibration was accomplished with dextrans of known average molecular weight (Mw range = 10,100-2,000,000). The elution volume of amylopectin (Ve = 2.5 ml) indicated that this starch component was fractionated on the column system despite its very large molecular size. Standard curves were prepared from various mixtures of purified corn and wheat amylose and amylopectin. From the linear relationships obtained, the percentages of both components in corn and wheat starches were determined. The method developed proved useful to monitor the purity of amylose and amylopectin preparations, and to estimate rapidly the amylose:amylopectin ratio of starch samples.

Amylopectin↗

PubMed1973

Amylopectin sulphate (SN-263) coats the gastric mucosal surface.

After the application in vitro of (14)C amylopectin sulphate solution to frozen sections of human ulcer-bearing stomach, autoradiography demonstrates localization of amylopectin sulphate to the gastric surface. The affinity of amylopectin sulphate macromolecule for the gastric luminal surface would provide a substrate-bound pepsin inhibitor with a molecular sieve-like action to exclude proteolytic enzymes from the mucosal surface. This protective coating action may mimic the hypothetical role of endogenous gastric mucous substances and account for the action of amylopectin sulphate in human peptic ulcer.

Amylopectin↗

PubMed1989

Diets containing high amylose vs amylopectin starch: effects on metabolic variables in human subjects.

Twelve men consumed a diet containing 34% of calories as 70% amylose or amylopectin starch to determine if the structure of starch could influence metabolic factors associated with abnormal states. Each starch was fed to subjects for 5 wk in a crossover design. No significant differences were observed in glucose or insulin levels when a glucose tolerance was given after 4 wk on each starch. However, glucose and insulin responses were significantly lower when a meal containing amylose compared with amylopectin was consumed after 5 wk on each starch. Summation of 0.5 through 2-h levels of insulin but not glucose were significantly lower after amylose compared with levels after amylopectin. Mean fasting triglyceride and cholesterol levels were significantly lower during the period when amylose was consumed. Long-term intake of dietary amylose may be valuable in decreasing insulin response while maintaining proper control of glucose tolerance and low levels of blood lipids.

Adult↗

PubMed1992

Waxy Chlamydomonas reinhardtii: monocellular algal mutants defective in amylose biosynthesis and granule-bound starch synthase activity accumulate a structurally modified amylopectin.

Amylose-defective mutants were selected after UV mutagenesis of Chlamydomonas reinhardtii cells. Two recessive nuclear alleles of the ST-2 gene led to the disappearance not only of amylose but also of a fraction of the amylopectin. Granule-bound starch synthase activities were markedly reduced in strains carrying either st-2-1 or st-2-2, as is the case for amylose-deficient (waxy) endosperm mutants of higher plants. The main 76-kDa protein associated with the starch granule was either missing or greatly diminished in both mutants, while st-2-1-carrying strains displayed a novel 56-kDa major protein. Methylation and nuclear magnetic resonance analysis of wild-type algal storage polysaccharide revealed a structure identical to that of higher-plant starch, while amylose-defective mutants retained a modified amylopectin fraction. We thus propose that the waxy gene product conditions not only the synthesis of amylose from endosperm storage tissue in higher-plant amyloplasts but also that of amylose and a fraction of amylopectin in all starch-accumulating plastids. The nature of the ST-2 (waxy) gene product with respect to the granule-bound starch synthase activities is discussed.

Alleles↗

PubMed1977

[Cytochemical study of different stages in the life cycle of Toxoplasma gondii. I. Amylopectin and lipids in endozoites].

Attempts were made to localize cytochemically acid micopolysaccharides, in addition to sulphate groups of mucosubstances in Toxoplasma endozoites of SS-119 and RH strains with negative results. Amylopectin was found to be the only polysaccharide so far detected in the endozoite stage, using the PAS technique. With RH strain toxoplasmas, the dynamics of amylopectin was followed within 6 days after mouse inoculation. On day 2, toxoplasmas and the host cells of the mouse peritoneal exudate being practically PAS-negative, the amount of amylopectin increased progressively towards day 6. The immune response of the host may be presumably involved in the pattern of this dynamics. Phospholipids were detected in the cytoplasm of intra- and extracellular endozoites of strain SS-119. Little, if any, amount of neutral fat was observed. Of special interest is the increased phospholipid content in the infected host cells.

Amylopectin↗

PubMed1977

The action pattern of human salivary alpha-amylase in the vicinity of the branch points of amylopectin.

Salivary alpha-amylase hydrolyses amylopectin in stages. At the end of the so-called second stage, there are present glucose, maltose, and a series of alpha-limit dextrins containing (1 leads to 4)- and (1 leads to 6)-alpha-D-glucosidic bonds. The structures of the limit dextrins containing a single (1 leads to 6)-bond were examined. Six such dextrins were found. Of these, two were capable of being further hydrolysed by alpha-amylase, whereas the remaining four were true, amylase-resistant alpha-limit dextrins. The structures of the limit dextrins afforded information about those (1 leads to 4)-alpha-D-glucosidic bonds of amylopectin that are capable of being cleaved by salivary alpha-amylase and those that are resistant. In order to define further the action of alpha-amylase, the alpha-amylolytic products of 6-alpha-maltotriosyl-D-glucose, 6(3)-alpha-maltotriosylmaltotriose, and 6(3)-alpha-maltotriosylmaltotetraose were examined.

Amylases↗

PubMed1973

Observations of the action of limit dextrinases on amylopectin-like polysaccharides.

The rate of hydrolysis of amylopectin by three different limit dextrinase preparations is only about 15-23% of that of amylopectin beta-limit dextrin under similar conditions. On dilution of the enzymes there was no change in specificity. The factors controlling the specificity of the enzyme and the possible significance in vivo of the results are discussed.

Chromatography, Gel↗

PubMed1991

Investigation of the fine structure of alpha-dextrins derived from amylopectin and their relation to the structure of waxy-maize starch.

Alpha-dextrins, obtained by fractional precipitation with methanol of the products of the action of Bacillus subtilis alpha-amylase on waxy-maize amylopectin, were debranched with isoamylase and the distributions of the unit chains were analysed by gel-permeation chromatography. The large alpha-dextrins still contained long B-chains after hydrolysis for 60 min, but these were absent from the small dextrins with chain numbers of approximately 11 or less. The small dextrins contained increased amounts of chains with lengths intermediate of those of the long B-chains and the main part of the short chains. After hydrolysis for 210 min, almost all of the long B-chains had disappeared and the chains with intermediate lengths had been shortened further. The distributions of the unit chains of the internal chains, obtained by debranching of the phosphorolysis (phi)-limit dextrins, gave similar results and showed that the ratio of A- to B-chains was unchanged during the alpha-amylolysis. Models for the fine structure of the intermediate alpha-dextrins are proposed.

Amylopectin↗

PubMed1989

Effect of water as a diluent on the glass transition behaviour of malto-oligosaccharides, amylose and amylopectin.

The glass transition behaviour of amorphous malto-oligomers from dimer to hexamer was investigated as a function of diluent (water) concentration using differential scanning calorimetry. The glass transition temperatures of the pure compounds ranged from 364 K for maltose to 448 K for maltohexaose. At low diluent concentrations the addition of water strongly depressed Tg. From the measurement of Tg and the heat capacity increment, delta Cp, of the transition for the pure compounds it was possible to predict the Tg of the malto-oligomer/water mixtures using a thermodynamic approach developed by Couchman. From the measurements on the malto-oligomers it was possible to obtain, by extrapolation, the high DP limits of delta Cp and Tg, which are appropriate to amylose and amylopectin. The predicted variation of Tg with diluent concentration for these materials was compared with the experimentally observed behaviour.

Amylopectin↗

PubMed1989

Conformational analysis and molecular modelling of the branching point of amylopectin.

The conformational properties of 6(2) alpha-D-glucosylmaltotriose have been studied using energy calculations that include van der Waals interactions, hydrogen bond stabilization, exo-anometric effect and torsional potential contributions. The calculations focused mainly on the conformational properties displayed at the alpha(1----6) linkage within the tetrasaccharide for which the conformational space is reported. The tetrasaccharide molecule was then considered as a model compound of the branching point in amylopectin. From molecular modelling, some basic structural features associated with branching were clearly established. It was found that, among the low energy arrangements, the side chain would fold back onto the main backbone, thereby producing dense three-dimensional structures in which a 'parallel' arrangement is achieved. The branching between two strands of the double helix, as found in the crystalline moiety of A and B starches, was further investigated. It was found that one particular set of conformations about the glycosidic linkages in the two different strands, could result in an arrangement such that strands could be connected through an alpha(1----6) glycosidic linkage, with a minimum of distortion. The three-dimensional features derived from the molecular modelling agree with the physical properties and mode of biogenesis within the starch granule; they are in accord with a 'cluster' type of structure.

Amylopectin↗

PubMed1990

Systematic conformational search for the branching point of amylopectin.

A systematic modelling for the branching point of amylopectin, on the basis of the double-helical structure proposed for amylose polymorphs was performed. A 'several steps' approach was used with increasing sophistication in the refinement, combining the use of geometrical criteria and molecular mechanics calculations. This modelling leads to four groups of solutions which were compared with those existing for amylose and the related oligomers. The most stable conformations provide a minimum of deformations for the alpha(1-4) linkages adjacent to the branching point. The conformation of minimum energy roughly corresponds to the proposal of Imberty and Perez and includes an alpha(1-6) configuration compatible with the well-known calculated maps. The other possible solutions are discussed in terms of deformations for the glucopyranose rings and of unusual conformation domains for the alpha(1-6) linkage.

Amylopectin↗

PubMed1988

A simple preparative method for the isolation of amylose and amylopectin from potato starch.

The defatted starch was dispersed in NaOH (1 M) and neutralized with HCl (1 M). The amylose 1-butanol complex is adsorbed on defatted cellulose powder in the solvent system containing acetate buffer (pH 4.8,0.1 M) + urea (2 M) + 1-butanol (8.5%, v/v). The complex adsorbed on cellulose powder is separated by centrifugation (2418 g). The sediment is washed with the solvent system-I to obtain the intermediate fraction. The adsorbed amylose is eluted with urea (2 M) in acetate buffer (pH 4.8, 0.1 M). The amylose, intermediate fraction and amylopectin were precipitated with ethanol, washed free of urea and air dried. They were characterized by determining their blue value and beta -amylolysis limit.

Amylopectin↗

PubMed1992

Amylose-amylopectin ratio in a meal affects postprandial variables in male volunteers.

To study the postprandial effects of changing the amylose-to-amylopectin ratio (Am:Ap) in the starch fraction of a meal, male volunteers were given hot mixed lunches (13% of energy as protein, 24% as fat, 6% as mono- and disaccharides, and 57% as polysaccharides) in which Am:Ap was either 0:100 or 45:55. The increase in Am:Ap resulted in a change in the shape of the glucose and insulin responses in the blood with significantly lower initial responses but a small increase for glucose and a decrease for insulin if averaged over the 6 h of the study. The rises in the concentration of free glycerol and free fatty acid that occurred after an initial drop were stronger at low Am:Ap. High-Am:Ap meals induced more satiety up to 6 h postprandially. There was no effect of Am:Ap on postprandial triacylglycerol in the blood or on breath hydrogen except for a weak trend toward a higher concentration at 6 h after the high-Am:Ap meals.

Adult↗

PubMed1978

Plasma clearance and renal excretion of erythrocyte cryoprotectant hydroxyethylated amylopectin.

The value of low molecular weight-hydroxyethylated amylopectin (cryo-HES) as an extracellular cryoprotectant has been demonstrated in vitro. It is important that details of the intravascular persistence and urinary excretion be determined to compare with data already available as other grades of HES and with data on transfusion of cryo-HES cryoprotected blood. Following a single 400 ml (14% solution) infusion in man, the intravascular clearance of cryo-HES was well described mathematically by the equation: y = 3.30+6.49e-0.15kappa. The plasma concentration of cryo-HES fell to half its peak value in approximately 9.6 h. Approximately 20% of the total infused cryo-HES was excreted in the urine during the first post-injection hour, and 50% by 72 h. The ESR was not altered significantly by the presence of this material. The present study indicates that cryo-HES is eliminated rapidly and may thus be safe for transfusion to recipients of frozen blood.

Adult↗