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  • 1
    Digitale Medien
    Digitale Medien
    PHYSICOCHEMICAL AND STRUCTURAL CHARACTERISTICS OF SODIUM CASEINATE BIOPOLYMERS INDUCED BY MICROBIAL TRANSGLUTAMINASE (2005)
    Oxford, UK and Malden, USA : Blackwell Science Inc
    Journal of food biochemistry 29 (2005), S. 0 
    Details
    ISSN: 1745-4514
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Some physicochemical properties and structural characteristics of microbial transglutaminase (MTGase)-induced biopolymers of sodium caseinate (SC) were investigated. The sodium dodecyl sulfate–polyacrylamide gel electrophoresis and size-exclusion–high-performance liquid chromatography analyses showed that all components of SC were easily polymerized or transformed by MTGase to form high-molecular weight biopolymers, and the susceptibility order of individual components was κ-Casein (C) 〉 α-C 〉 β-C. The emulsifying properties of biopolymers depended on the incubation time with MTGase. The emulsifying activity index of biopolymers persistently increased with the MTGase (0–12 h) incubation time. The emulsion stability also increased with the incubation time (〈 4 h), then declined a little with longer incubation (4–12 h). The differential scanning calorimetry analysis showed that the thermal properties of the biopolymers obtained after a 12-h incubation were different from that of native SC or biopolymers obtained after a shorter incubation time (〈 4 h), suggesting that the former has higher thermal stability. In addition, the ultraviolet (UV) spectra showed that the UV absorbance (at 275 nm) of MTGase-induced biopolymers of SC decreased with an increasing incubation time with MTGase, and the maximal emission wavelength (λ max ) slightly shifted to the “blue side.” The fluorescence spectra showed that the λ max was related with incubation time with MTGase, slightly shifting to the “blue side” after 4 h with no further changes; its relative fluorescence intensity also increased. These results suggest a relationship between the functionalities and structural characteristics of the MTGase-induced biopolymers of SC.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1745-4514.2005.00038.x
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  • 2
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    Regulation of trehalase expression inhibits apoptosis in diapause cysts of Artemia (2013)
    Portland Press
    Details
    Publikationsdatum: 2013-11-09
    Beschreibung: Trehalase, which specifically hydrolyses trehalose into glucose, plays an important role in the metabolism of trehalose. Large amounts of trehalose are stored in the diapause encysted embryos (cysts) of Artemia , which are not only vital to their extraordinary stress resistance, but also provide a source of energy for development after diapause is terminated. In the present study, a mechanism for the transcriptional regulation of trehalase was described in Artemia parthenogenetica . A trehalase-associated protein (ArTAP) was identified in Artemia -producing diapause cysts. ArTAP was found to be expressed only in diapause-destined embryos. Further analyses revealed that ArTAP can bind to a specific intronic segment of a trehalase gene. Knockdown of ArTAP by RNAi resulted in the release of cysts with coarse shells in which two chitin-binding proteins were missing. Western blotting showed that the level of trehalase was increased and apoptosis was induced in these ArTAP-knockdown cysts compared with controls. Taken together, these results show that ArTAP is a key regulator of trehalase expression which, in turn, plays an important role in trehalose metabolism during the formation of diapause cysts.
    Print ISSN: 0264-6021
    Digitale ISSN: 0006-2936
    Thema: Biologie , Chemie und Pharmazie
    Publiziert von Portland Press im Namen von The Biochemical Society.
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  • 3
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    Crystal structures of S6K1 provide insights into the regulation mechanism of S6K1 by the hydrophobic motif (2013)
    Portland Press
    Details
    Publikationsdatum: 2013-07-30
    Beschreibung: The activity of S6K1 (p70 ribosomal protein subunit 6 kinase 1) is stimulated by phosphorylation of Thr 389 in the hydrophobic motif by mTORC1 (mammalian target of rapamycin complex 1) and phosphorylation of Thr 229 in the activation loop by PDK1 (phosphoinositide-dependent kinase 1); however, the order of the two events is still ambiguous. In the present paper we report six crystal structures of the S6K1 kinase domain alone or plus the hydrophobic motif in various forms, in complexes with a highly specific inhibitor. The structural data, together with the biochemical data, reveal in vivo phosphorylation of Thr 389 in the absence of Thr 229 phosphorylation and demonstrate the importance of two conserved residues, Gln 140 and Arg 121 , in the establishment of a hydrogen-bonding network between the N-lobe (N-terminal lobe) and the hydrophobic motif. Phosphorylation of Thr 389 or introduction of a corresponding negatively charged group leads to reinforcement of the network and stabilization of helix αC. Furthermore, comparisons of S6K1 with other AGC (protein kinase A/protein kinase G/protein kinase C) family kinases suggest that the structural and sequence differences in the hydrophobic motif and helix αC account for their divergence in PDK1 dependency. Taken together, the results of the present study indicate that phosphorylation of the hydrophobic motif in S6K1 is independent of, and probably precedes and promotes, phosphorylation of the activation loop.
    Print ISSN: 0264-6021
    Digitale ISSN: 0006-2936
    Thema: Biologie , Chemie und Pharmazie
    Publiziert von Portland Press im Namen von The Biochemical Society.
    Standort Signatur Einschränkungen Verfügbarkeit
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