ISOLATION AND CHARACTERIZATION OF RAT SKELETAL-MUSCLE PROTEOGLYCAN DECORIN AND COMPARISON WITH THE HUMAN FIBROBLAST DECORIN

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dc.contributor.authorANDRADE, W
dc.contributor.authorBRANDAN, E
dc.date.accessioned2025-01-23T19:22:51Z
dc.date.available2025-01-23T19:22:51Z
dc.date.issued1991
dc.description.abstract1. The extracellular matrix (ECM) of rat skeletal muscle contains several proteoglycans (PGs). The more abundant correspond to a chondroitin/dermatan sulfate PG or decorin.
dc.description.abstract2. Decorin isolated from rat skeletal muscle ECM has a smaller molecular size than human fibroblast decorin.
dc.description.abstract3. The difference in size is mainly due to the glycosaminoglycan (GAG) chain length rather than the core protein size.
dc.description.abstract4. Peptide analysis of trypsin treated decorins shows at least three peptides with the same electrophoretic mobility.
dc.fuente.origenWOS
dc.identifier.eissn1879-1107
dc.identifier.issn1096-4959
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/99116
dc.identifier.wosidWOS:A1991GY82600021
dc.issue.numero3
dc.language.isoen
dc.pagina.final570
dc.pagina.inicio565
dc.revistaComparative biochemistry and physiology b-biochemistry & molecular biology
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleISOLATION AND CHARACTERIZATION OF RAT SKELETAL-MUSCLE PROTEOGLYCAN DECORIN AND COMPARISON WITH THE HUMAN FIBROBLAST DECORIN
dc.typeartículo
dc.volumen100
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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