| Literature DB >> 29446773 |
Héctor Capella-Monsonís1,2, João Q Coentro1,2, Valeria Graceffa1,2, Zhuning Wu1,2, Dimitrios I Zeugolis1,2.
Abstract
Collagen type I is the most abundant extracellular matrix protein, and collagen type I supramolecular assemblies (e.g., tissue grafts, biomaterials and cell-assembled systems) are used extensively in tissue engineering and regenerative medicine. Many studies, for convenience or economic reasons, do not accurately determine collagen type I purity, concentration, solubility and extent of cross-linking in biological specimens, frequently resulting in erroneous conclusions. In this protocol, we describe solubility; normal, reduced and delayed (interrupted) SDS-PAGE; hydroxyproline; Sircol collagen and Pierce BCA protein; denaturation temperature; ninhydrin/trinitrobenzene sulfonic acid; and collagenase assays and assess them in a diverse range of biological samples (e.g., tissue samples; purified solutions or lyophilized materials; 3D scaffolds, such as sponges and hydrogels; and cell media and layers). Collectively, the described protocols provide a comprehensive, yet fast and readily implemented, toolbox for collagen type I characterization in any biological specimen.Entities:
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Year: 2018 PMID： 29446773 DOI： 10.1038/nprot.2017.117
Source DB: PubMed Journal: Nat Protoc ISSN： 1750-2799 Impact factor: 13.491