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Transglutaminase -induced

Junn, E., Ronchetti, R. D., Quezado, M. M., Kim, S. Y., and Mouradian, M. M. (2003). Tissue transglutaminase-induced aggregation of alpha-synuclein Implications for Lewy body formation in Parkinson s disease and dementia with Lewy bodies. Proc. Natl. Acad. Sci. USA 100, 2047-2052. [Pg.142]

Autio, K., Kruus, K., Knaapila, A., Gerber, N., Flander, L., Buchert, J. 2005. Kinetics of transglutaminase-induced cross-linking of wheat proteins in dough. J Agric Food Chem 53 1039-1045. [Pg.308]

Schorsch, C., Carrie, H., Clark, A.H., and Norton, l.T. (2000a). Cross-linking casein micelles by a microbial transglutaminase conditions for formation of transglutaminase-induced gels. Int. Dairy J. 10, 519-528. [Pg.36]

Hartley DM, Zhao C, Speier AC, Woodard GA, Li S, Li Z, Walz T (2008) Transglutaminase induces protofibril-like amyloid beta-protein assemblies that are protease-resistant and inhibit long-term potentiation. J Biol Chem 283 16790-16800 Hashimoto M, Rockenstein E, Crews L, MasUah E (2003) Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer s and Parkinson s diseases. Neuromolecular Med 4 21-36... [Pg.314]

Zou, Q. Liu, X. Zhao, J. Tian, F. Zhang, H.-p. Zhang, H. Chen, W., Microencapsulation of Bifidobacterium bifidum F-35 in whey protein-based microcapsules by transglutaminase-induced gelation. Journal of Food Science (2012) 77, M270-M277. [Pg.799]

Heidebach, T., Forst, P., Kulozik, U. Transglutaminase-induced caseinate gelation for the microencapsulation of probiotic cells. Int. Dairy J. 19, 77-84 (2009)... [Pg.189]

The solubility of TG treated films was compared to that of non treated films (Fig 3). Films obtained with deamidated gluten were soluble at 78% in water, the addition of putrescine didn t modify the film solubility (Fig 3). The action of transglutaminase induced a decrease in the film water solubility. The highest insolubility was obtained for a ratio putrescine / glutamine of 0.18 mole/mole and could be related to the formation of polymers of high molecular weight. [Pg.249]

Bae, H.J., Darby, D.O., Kimmel, R.M., Park, H.J., and Whiteside, W.S. 2009. Effects of transglutaminase-induced cross-linking on properties of fish gelatin-nanoclay composite film. Food Chem. 114 180-189. [Pg.952]

Factor XIII. Factor XIII circulates in the blood as a zymogen composed of two pairs of different polypeptide chains designated A and B. Inert Factor XIII has a molecular weight of 350,000 daltons and is converted to its active transglutaminase form in the presence of thrombin and calcium. Activated Factor XIII, Xllla, induces an irreversible amide exchange reaction between the y-glutamine and S-lysine side chains of adjacent fibrin... [Pg.174]

An old hypothesis is based on the observations of Dahlen et al. (D3), who demonstrated that above a certain concentration in plasma, Lp(a) could bind to glycosaminoglycans in the arterial wall (B12). Colocalization of Lp(a) and fibrin on the arterial wall can lead to oxidative changes in the lipid moiety of Lp(a) and induce the formation of oxidatively modified cholesterol esters, which in turn can influence the interaction of Lp(a) and its receptors on macrophages. This process is promoted by the presence of calcium ions. Cushing (C14), Loscalzo (L22), and Rath (R3) reported a colocalization of undegraded Lp(a) and apo-Bl00 in the extracellular space of the arterial wall. In contrast to LDL, Lp(a) is a substrate for tissue transglutaminase and Factor XUIa and can be altered to products that readily interact with cell surface structures (B21). [Pg.96]

Kohno H, Hoshino Y, Katoh S, et al. 1992. Effect of retinoic acid on liver transglutaminase activity and carbon tetrachloride-induced liver damage in mice. Experientia 48 386-388. [Pg.170]

Feingold and his coworkers demonstrated an important role of nuclear hormone receptor on epidermal differentiation and stratum corneum barrier formation. Activation ofPPARa Peroxisome proliferator-activated receptor a by farnesol also stimulated the differentiation of epidermal keratinocytes.42 Cornified envelope formation, involcrin, and transglutaminase protein, and mRNA levels were also increased by the activation of PPARo . Interestingly, the inflammatory response was also inhibited by the treatment.43 They also showed that topical application of PPARo activators accelerated the barrier recovery after tape stripping or acetone treatment and prevented the epidermal hyperplasia induced by repeated barrier disruption.42 Regulation of the nuclear hormone receptor would open a new possibility for improvement of the cutaneous barrier. [Pg.112]

Palosuo, K., Varjonen, E., Nurkkala, J., Kalkkinen, N., Harvima, R., Reunala, T., Alenius, HJ. 2003. Transglutaminase-mediated cross-linking of a peptic fraction of omega-5 gliadin enhances IgE reactivity in wheat-dependent, exercise-induced anaphylaxis. J Allergy Clin Immunol 111 1386-1392. [Pg.314]

Mariani, P., Carsughi, F., Spinozzi, F., Romanzetti, S., Meier, G., Casadio, R. and Bergamini, C. M. (2000) Ligand-induced conformational changes in tissue transglutaminase Monte Carlo analysis of small-angle scattering data, Biophys. J. 78, 3240-3251. [Pg.211]

Figure 19.23. Transglutaminase (Tg)-induced cross-linking reaction between lysine and... Figure 19.23. Transglutaminase (Tg)-induced cross-linking reaction between lysine and...
Szondy, Z., Molnar, P., Nemes, Z., Boyiadzis, M, Kedei, N., Toth, R., and Fesus, L. (1997) Differential expression of tissue transglutaminase during in vivo apoptosis of thymocytes induced via distinct signalling pathways. FEBS Lett. 404, 307-313. [Pg.52]


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