المؤلفون: de Bruijn, Johannes, Martínez‐Oyanedel, José, Loyola, Cristina, Seiter, Javier, Lobos, Francisco, Pérez‐Arias, Ricardo

المصدر: International Journal of Food Science & Technology ; volume 46, issue 8, page 1691-1698 ; ISSN 0950-5423 1365-2621

الوصف: Summary After ultrafiltration (UF) thermally unstable compounds of Sauvignon blanc wines were concentrated in the retentate fractions of 10–30 kDa increasing heat‐induced haze 8.9‐fold, while concentrating haze stabilising species into the retentate fractions of 100–300 kDa with a 5.3‐fold reduction of heat‐induced haze compared to unfiltered wine. Proteins having molecular weights of 18, 23, 33, 35, 40 and 60 kDa were identified as the main haze promoting agents for Sauvignon blanc, where the proteins of 56, 69 and 72 kDa were identified as thermally stable. Potassium sulphate (100 mg L −1 ) and magnesium sulphate (25 mg L −1 ) did not affect wine haziness at experimental diafiltration (DF) conditions using model wine solutions. Combination of UF and DF is a useful separation method of wine proteins, which is helpful to quantify haziness of individual species and to reveal the interactions between species involving protein haze.

الإتاحة: https://doi.org/10.1111/j.1365-2621.2011.02667.xTest

المؤلفون: Sepúlveda-Ugarte, José, Brunet, Juan E., Matamala, Adelio R., Martínez-Oyanedel, José, Bunster, Marta

المصدر: Journal of Photochemistry and Photobiology A: Chemistry ; volume 219, issue 2-3, page 211-216 ; ISSN 1010-6030

مصطلحات موضوعية: General Physics and Astronomy, General Chemical Engineering, General Chemistry

الإتاحة: https://doi.org/10.1016/j.jphotochem.2011.02.012Test
https://api.elsevier.com/content/article/PII:S1010603011000748?httpAccept=text/xmlTest
https://api.elsevier.com/content/article/PII:S1010603011000748?httpAccept=text/plainTest

المؤلفون: McNae, Iain W., Martinez-Oyanedel, José, Keillor, Jeffrey W., Michels, Paul A.M., Fothergill-Gilmore, Linda A., Walkinshaw, Malcolm D.

المصدر: Journal of Molecular Biology ; volume 385, issue 5, page 1519-1533 ; ISSN 0022-2836

مصطلحات موضوعية: Molecular Biology, Structural Biology

الإتاحة: https://doi.org/10.1016/j.jmb.2008.11.047Test
https://api.elsevier.com/content/article/PII:S0022283608014782?httpAccept=text/xmlTest
https://api.elsevier.com/content/article/PII:S0022283608014782?httpAccept=text/plainTest

المؤلفون: Bruna, Carola, Arriagada, Gloria, Lian, Jane B., Stein, Gary S., Bunster, Marta, Martinez‐Oyanedel, Jose, Montecino, Martin

المصدر: Journal of Cellular Biochemistry ; volume 101, issue 3, page 785-789 ; ISSN 0730-2312 1097-4644

الوصف: The Runx2 transcription factor is a key regulator of osteoblast differentiation. In response to 1α,25 dihydroxy vitamin D3, Runx2 may interact with the 1α,25 dihydroxy vitamin D3 receptor (VDR) in the promoter of target genes, producing a synergic activation of their transcription. Previous studies have suggested that the motifs responsible for the VDR–Runx2 interaction are contained within the 230–361 domain of Runx2. In this work, we confirmed by GST‐pull down that Runx2 I(209–361) is sufficient to interact with the VDR. To obtain structural information, GST–Runx2 I(209–361) protein was overexpressed in Escherichia coli , purified and crystallized using the hanging‐drop vapor‐diffusion method and polyethyleneglycol as a precipitant. The crystals were found to diffract to a maximum resolution of 2.7 Å and a complete data set to a 3.3 Å resolution was collected and analyzed. The crystals belong to the tetragonal system, with a space group P 4 and unit‐cell parameters of a = b = 90.8, and c = 57.2 Å. The presence of a monomer of the recombinant GST–Runx2 I(209–361) in the asymmetric unit gives a V M of 2.7 Å 3 Da −1 and a solvent content of 54.8%. J. Cell. Biochem. 101: 785–789, 2007. © 2007 Wiley‐Liss, Inc.

الإتاحة: https://doi.org/10.1002/jcb.21231Test

المؤلفون: Martinez-Oyanedel, José, McNae, Iain W., Nowicki, Matthew W., Keillor, Jeffrey W., Michels, Paul A.M., Fothergill-Gilmore, Linda A., Walkinshaw, Malcolm D.

المصدر: Journal of Molecular Biology ; volume 366, issue 4, page 1185-1198 ; ISSN 0022-2836

مصطلحات موضوعية: Molecular Biology, Structural Biology

الإتاحة: https://doi.org/10.1016/j.jmb.2006.10.019Test
https://api.elsevier.com/content/article/PII:S0022283606013581?httpAccept=text/xmlTest
https://api.elsevier.com/content/article/PII:S0022283606013581?httpAccept=text/plainTest

المؤلفون: Vorphal, María, Bruna, Carola, Wandersleben, Traudy, Dagnino-Leone, Jorge, Lobos-González, Francisco, Uribe, Elena, Martínez-Oyanedel, José, Bunster, Marta

المصدر: Biological Research; December 2017, Vol. 50 Issue: 1 p1-10, 10p

مستخلص: Ferredoxin NADP(H) oxidoreductases (EC 1.18.1.2) (FNR) are flavoenzymes present in photosynthetic organisms; they are relevant for the production of reduced donors to redox reactions, i.e. in photosynthesis, the reduction of NADP+to NADPH using the electrons provided by Ferredoxin (Fd), a small FeS soluble protein acceptor of electrons from PSI in chloroplasts. In rhodophyta no information about this system has been reported, this work is a contribution to the molecular and functional characterization of FNR fromGracilaria chilensis, also providing a structural analysis of the complex FNR/Fd. The biochemical and kinetic characterization of FNR was performed from the enzyme purified from phycobilisomes enriched fractions. The sequence of the gene that codifies for the enzyme, was obtained using primers designed by comparison with sequences ofSynechocystisand EST fromGracilaria. 5′RACE was used to confirm the absence of a CpcD domain in FNRPBS ofGracilaria chilensis. A three dimensional model for FNR and Fd, was built by comparative modeling and a model for the complex FNR: Fd by docking. The kinetic analysis shows KMNADPHof 12.5 M and akcatof 86 s−1, data consistent with the parameters determined for the enzyme purified from a soluble extract. The sequence for FNR was obtained and translated to a protein of 33646 Da. A FAD and a NADP+ binding domain were clearly identified by sequence analysis as well as a chloroplast signal sequence. Phycobilisome binding domain, present in some cyanobacteria was absent. Transcriptome analysis ofGchrevealed the presence of two Fd; FdL and FdS , sharing the motif CX5CX2CX29X. The analysis indicated that the most probable partner for FNR is FdS. The interaction model produced, was consistent with functional properties reported for FNR in plants leaves, and opens the possibilities for research in other rhodophyta of commercial interest.

المؤلفون: Sivakumar, Radhakrishnan, Manivel, Arumugam, Melendrez, Manuel, Martinez-Oyanedel, José, Bunster-Balocchi, Marta Cecilia Del Carmen, Vergara, Carola, Manidurai, Paulraj

المصدر: Polyhedron

الوصف: Two novel heteroleptic ruthenium (II) sensitizers S1 and S2 containing an ancillary ligand 9,9-bis(9-ethylcarbazol-3-yl)-4,5-diazafluorene and 9,9-bis(9-phenylcarbazol-3-yl)-4,5-diazafluorene respectively, have been synthesized and characterized by H-1 NMR, UVVis absorption spectroscopy, mass spectrometry, elemental analysis and cyclic voltammetry, and used as sensitizers in dye sensitized solar cells. The results show that for the two ruthenium sensitizers, the introduction of carbazole via sp(3) hybridized C9 atom of the 4,5-diazafluorene unit produces significant changes in their optical absorption spectra and subsequently alters the intra-molecular charge transfer processes that influence the photovoltaic performance of the solar cell device. The power conversion efficiency of dye sensitized solar cells fabricated using sensitizers S1 and S2 are 0.36% and 0.42% respectively, while N719 exhibits 3.6% under the same device fabrication and measuring conditions. (C) 2014 Elsevier Ltd. All rights reserved.

العلاقة: instname: Conicyt; reponame: Repositorio Digital RI2.0; info:eu-repo/grantAgreement//1130256; info:eu-repo/semantics/dataset/hdl.handle.net/10533/93477; http://hdl.handle.net/10533/215547Test; wos: WOS:000353316800017

الإتاحة: https://doi.org/10.1016/j.poly.2014.11.008Test
http://hdl.handle.net/10533/215547Test

المؤلفون: Vorphal, María Alejandra, Gallardo-Escarate, Cristian, Valenzuela-Muñoz, Valentina, Dagnino-Leone, Jorge, Vasquez, Jose Aleikar, Martinez-Oyanedel, José, Bunster-Balocchi, Marta Cecilia Del Carmen

المصدر: Marine Genomics

الوصف: This work reports the results of the Illumina RNA-Seq of a wild population of female haploid plants of Gracilaria chilensis (Bird et al., 1986) (Rhodophyta, Gigartinalis). Most transcripts Were de novo assembled in 12,331 contigs with an average length of 1756 bp, showing that 96.64% of the sequences were annotated with known proteins. In particular, the identification of linker proteins of phycobilisomeS (PBS) is reported. Linker proteins have primary been identified in cyanobacteria but the information available about them in eukaryotic red alga is not complete, and this is the first report in G. chilensis. This resource will also provide the basis for the study of metabolic pathways related to polysaccharide production. (C) 2016 Elsevier B.V. All rights reserved

العلاقة: instname: Conicyt; reponame: Repositorio Digital RI2.0; info:eu-repo/grantAgreement//1130256; info:eu-repo/semantics/dataset/hdl.handle.net/10533/93477; http://hdl.handle.net/10533/215548Test; wos: WOS:000394081500004

الإتاحة: https://doi.org/10.1016/j.margen.2016.11.001Test
http://hdl.handle.net/10533/215548Test

المؤلفون: de Bruijn, Johannes, Martinez-Oyanedel, Jose, Loyola, Cristina, Lobos, Francisco, Seiter, Javier, Perez, Ricardo

المصدر: JOURNAL INTERNATIONAL DES SCIENCES DE LA VIGNE ET DU VIN

جغرافية الموضوع: fra, TALENCE

العلاقة: instname: Conicyt; reponame: Repositorio Digital RI2.0; info:eu-repo/grantAgreement/Fondecyt/11085054; info:eu-repo/semantics/dataset/hdl.handle.net/10533/93477; http://hdl.handle.net/10533/143500Test; wos: WOS:000295487100006

الإتاحة: http://hdl.handle.net/10533/143500Test

المؤلفون: de Bruijn, Johannes, Martinez-Oyanedel, Jose, Loyola, Cristina, Seiter, Javier, Lobos, Francisco, Perez-Arias, Ricardo

المصدر: INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY

جغرافية الموضوع: usa, MALDEN

العلاقة: instname: Conicyt; reponame: Repositorio Digital RI2.0; info:eu-repo/grantAgreement/Fondecyt/11085054; info:eu-repo/semantics/dataset/hdl.handle.net/10533/93477; http://hdl.handle.net/10533/136543Test; wos: WOS:000292520500019

الإتاحة: https://doi.org/10.1111/j.1365-2621.2011.02667.xTest
http://hdl.handle.net/10533/136543Test