Abstract
Fibrocartilage of bovine knee meniscus was analyzed for major and minor collagen constituents. The main fraction (∼98%) of pepsin‐solubilized collagen consisted of type I with a small proportion (< 10%) of type III molecules. The minor fraction (1–2%) isolated by salt precipitation could be further resolved into type V collagen that consisted of α1(V) and α2(V) chains and a type II‐like molecule with chains that had all the characteristics of the 3α variant of α1(II) found in hyaline cartilage. The articular surface zone of the meniscus appeared 2–3‐fold enriched in these minor collagens compared with deeper tissue, though qualitatively the same distinctive collagen phenotype was evident throughout.
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