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Poly extracellular

Galactosylated chitosan prepared from lactobionic acid and chitosan with l-ethyl-3-(3-dimethylaminopropyl)-carbodiimideand N-hydroxysuccinimide was a good extracellular matrix for hepatocyte attachment [155] (Fig. 4). Furthermore, graft copolymers of galactosylated chitosan with poly(ethylene glycol) or poly(vinyl pyrrolidone) were useful for hepatocyte-targeting DNA carrier [156,157]. [Pg.170]

Mutans streptococci are the major pathogenic organisms of dental caries in humans. The pathogenicity is closely related to production of extracellular, water-insoluble glucans from sucrose by glucosyltransferase and acid release from various fermentable sugars. Poly(catechin) obtained by HRP catalyst in a phosphate buffer (pH 6) markedly inhibited glucosyltransferase from Streptococcus sorbrinus 6715, whereas the inhibitory effect of catechin for this enzyme was very low. [Pg.242]

Collmer A, Batemann DF (1982) Regulation of extracellular pectate lyase in Erwinia chrysanthemi. evidence that reaction products of pectate lyase and exo-poly-a-D-galacturonase mediate induction on galacturonan. Physiol Plant Pathol 21 127-139... [Pg.396]

An extracellular enzyme from Xanthomonas sp. is able to degrade poly(c -l,4-isoprene) with the production of 12-keto-4,8-dimethyltrideca-4,8-diene-l-al (Braaz et al. 2004), and functions as a heme-dependent oxygenase (Braaz et al. 2005). [Pg.305]

Dextran is the collective name of extracellular bacterial poly-alpha-D-glucopyranoses linked largely by 1,6 bonds, with branching occurring at the 1,2, 1,3 or 1,4 bonds. Physical properties vary... [Pg.426]

Synthetic Polymers. Synthetic polymers are versatile and offer promise for both targeting and extracellular-intracellular drug delivery. Of the many soluble synthetic polymers known, the poly(amino acids) [poly(L-lysine), poly(L-aspartic acid), and poly(glutamic acid)], poly(hydroxypropylmethacrylamide) copolymers (polyHPMA), and maleic anhydride copolymers have been investigated extensively, particularly in the treatment of cancers. A brief discussion of these materials is presented. [Pg.573]

Polyesters, such as microbially produced poly[(P)-3-hydroxybutyric acid] [poly(3HB)], other poly[(P)-hydroxyalkanoic acids] [poly(HA)] and related biosynthetic or chemosynthetic polyesters are a class of polymers that have potential applications as thermoplastic elastomers. In contrast to poly(ethylene) and similar polymers with saturated, non-functionalized carbon backbones, poly(HA) can be biodegraded to water, methane, and/or carbon dioxide. This review provides an overview of the microbiology, biochemistry and molecular biology of poly(HA) biodegradation. In particular, the properties of extracellular and intracellular poly(HA) hydrolyzing enzymes [poly(HA) depolymerases] are described. [Pg.289]

Extracellular Degradation of Polymers Related to Bacterial Poly(HA) 316... [Pg.289]

Identification and Isolation of Extracellular Poly(HA)-Degrading Microorganisms... [Pg.291]

The ability to degrade extracellular poly(HA) is widely distributed among bacteria and fungi and depends on the secretion or surface-display of specific... [Pg.292]

Extracellular, exo-type poly(/3-L-malic acid) hydrolase 124... [Pg.297]

Brandi et al. [71] using culture fluid of Acidovorax delafieldii and cyclic 3HB oligomers were in agreement with the presence of endo-hydrolase activity of poly(3HB) depolymerases. Similar results were obtained by de Koning et al. [72] who demonstrated that covalently cross-linked poly(HAMCL) was hydrolyzed completely by P. fluorescens. It is assumed that most - if not all - extracellular poly(HA) depolymerases have endo- and exo-hydrolase activity. Depending on the depolymerase the hydrolysis products are only monomers, monomers and dimers, or a mixture of oligomers (mono- to trimers). [Pg.308]

The i-poly(3HB) depolymerase of R. rubrum is the only i-poly(3HB) depolymerase that has been purified [174]. The enzyme consists of one polypeptide of 30-32 kDa and has a pH and temperature optimum of pH 9 and 55 °C, respectively. A specific activity of 4 mmol released 3-hydroxybutyrate/min x mg protein was determined (at 45 °C). The purified enzyme was inactive with denatured poly(3HB) and had no lipase-, protease-, or esterase activity with p-nitro-phenyl fatty acid esters (2-8 carbon atoms). Native poly(3HO) granules were not hydrolyzed by i-poly(3HB) depolymerase, indicating a high substrate specificity similar to extracellular poly(3HB) depolymerases. Recently, the DNA sequence of the i-poly(3HB) depolymerase of R. eutropha was published (AB07612). Surprisingly, the DNA-deduced amino acid sequence (47.3 kDa) did not contain a lipase box fingerprint. A more detailed investigation of the structure and function of bacterial i-poly(HA) depolymerases will be necessary in future. [Pg.316]

A different pH-triggered deshielding concept with hydrophilic polymers is based on reversing noncovalent electrostatic bonds [78, 195, 197]. For example, a pH-responsive sulfonamide/PEl system was developed for tumor-specific pDNA delivery [195]. At pH 7.4, the pH-sensitive diblock copolymer, poly(methacryloyl sulfadimethoxine) (PSD)-hZocA -PEG (PSD-b-PEG), binds to DNA/PEI polyplexes and shields against cell interaction. At pH 6.6 (such as in a hypoxic extracellular tumor environment or in endosomes), PSD-b-PEG becomes uncharged due to sulfonamide protonation and detaches from the nanoparticles, permitting PEI to interact with cells. In this fashion PSD-b-PEG is able to discern the small difference in pH between normal and tumor tissues. [Pg.12]

Figure 4.10. Dose-relationships for histamine release from rat mast cells induced by a variety of peptides [99], No calcium was added to the extracellular medium. Each point is the mean of two or more determinations A, poly(L-lysine) (molecular weight 30.000-70,000) , succinylated poly(L-lysine) (molecular weight 30,000-70f)00) V, [n-Phe7 )SP , fD-Prcr2, D-Phe7, D-Trpv]SP, u , SP/ A, eledoisin-related peptide , eledoisin O, N-terminal tetrapeptide of substance P. Figure 4.10. Dose-relationships for histamine release from rat mast cells induced by a variety of peptides [99], No calcium was added to the extracellular medium. Each point is the mean of two or more determinations A, poly(L-lysine) (molecular weight 30.000-70,000) , succinylated poly(L-lysine) (molecular weight 30,000-70f)00) V, [n-Phe7 )SP , fD-Prcr2, D-Phe7, D-Trpv]SP, u , SP/ A, eledoisin-related peptide , eledoisin O, N-terminal tetrapeptide of substance P.

See other pages where Poly extracellular is mentioned: [Pg.296]    [Pg.298]    [Pg.482]    [Pg.790]    [Pg.232]    [Pg.242]    [Pg.137]    [Pg.53]    [Pg.35]    [Pg.77]    [Pg.83]    [Pg.289]    [Pg.289]    [Pg.290]    [Pg.291]    [Pg.291]    [Pg.291]    [Pg.291]    [Pg.291]    [Pg.298]    [Pg.299]    [Pg.299]    [Pg.303]    [Pg.304]    [Pg.305]    [Pg.309]    [Pg.309]    [Pg.311]    [Pg.315]    [Pg.316]    [Pg.487]    [Pg.144]    [Pg.362]    [Pg.105]    [Pg.166]   
See also in sourсe #XX -- [ Pg.294 ]




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