dc.creatorTomiosso, TC
dc.creatorGomes, L
dc.creatorVidal, BD
dc.creatorPimentel, ER
dc.date2005
dc.date2014-11-13T22:29:34Z
dc.date2015-11-26T17:11:50Z
dc.date2014-11-13T22:29:34Z
dc.date2015-11-26T17:11:50Z
dc.date.accessioned2018-03-29T00:00:18Z
dc.date.available2018-03-29T00:00:18Z
dc.identifierBiocell. Inst Histol Embriol-conicet, v. 29, n. 1, n. 47, n. 54, 2005.
dc.identifier0327-9545
dc.identifierWOS:000229197300007
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/66555
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/66555
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/66555
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1281192
dc.descriptionThe composition and organization of the extracellular matrix of ostrich articular cartilage was investigated, using samples from the proximal and distal surfaces of the tarsometatarsus. For morphological analysis, sections were stained with toluidine blue and analyzed by polarized light microscopy. For biochemical analysis, extracellular matrix components were extracted with 4 M guanidinium chloride, fractionated on DEAF-Sephacel and analyzed by SDS-PAGE. Glycosaminoglycans were analyzed by electrophoresis in agarose gels. Structural analysis showed that the fibrils were arranged in different directions, especially on the distal surface. The protein and glycosaminoglycan contents of this region were higher than in the other regions. SDS-PAGE showed the presence of proteins with molecular masses ranging from 17 to 121 kDa and polydisperse components of 67, 80-100, and 250-300 kDa in all regions. The analysis of glycosaminoglycans in agarosepropylene diamine gels revealed the presence of only chondroitin-sulfate. The electrophoretic band corresponding to putative decorin was a small proteoglycan containing chondroitin-sufate and not dermatan-sulfate, unlike other cartilages. The higher amounts of proteins and glycosaminoglycans and the multidirectional arrangement of fibrils seen in the distal region may be correlated with the higher compression normally exerted on this region.
dc.description29
dc.description1
dc.description47
dc.description54
dc.languageen
dc.publisherInst Histol Embriol-conicet
dc.publisherMendoza
dc.publisherArgentina
dc.relationBiocell
dc.relationBiocell
dc.rightsaberto
dc.sourceWeb of Science
dc.subjectarticular cartilage
dc.subjectcollagen
dc.subjectdecorin
dc.subjectostrich
dc.subjectproteoglycan
dc.subjectCollagen-ii
dc.subjectProteoglycans
dc.subjectMacromolecules
dc.subjectQuantitation
dc.subjectProteins
dc.subjectBehavior
dc.subjectDecorin
dc.subjectBiology
dc.subjectTissues
dc.titleExtracellular matrix of ostrich articular cartilage
dc.typeArtículos de revistas


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