Structural and functional comparison of type IX collagen-proteoglycan from chicken cartilage and vitreous humor.

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Structural and functional comparison of type IX collagen-proteoglycan from chicken cartilage and vitreous humor.

Type IX collagen-proteoglycan is a major component of hyaline cartilages where it is located on the surface of the collagen fibrils so that a collagenous domain of the molecule (called COL3) and a non-collagenous domain (called NC4) project at periodic distances away from the surface of the fibril. Type IX collagen-proteoglycan is also present on the surface of the collagen fibrils of the adult...

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Occurrence in chick embryo vitreous humor of a type IX collagen proteoglycan with an extraordinarily large chondroitin sulfate chain and short alpha 1 polypeptide.

We have prepared a high buoyant density proteoglycan fraction from the vitreous humor of 13-day-old chick embryos. Using immunoblot analysis coupled with chondroitinase digestion, we demonstrate that the purified preparation is composed predominantly of type IX collagen-like chondroitin sulfate proteoglycan with an alpha 1(IX) chain Mr approximately 23,000 shorter than the known alpha 1 in cart...

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Vitreous structure. V. The morphology and thermal stability of vitreous collagen fibers and comparison to articular cartilage (type II) collagen.

Vitreous samples from bovine, ovine, human, canine, and lapine unfrozen eyes were found to contain fine fibrils which displayed no clearly discernible banding pattern when negatively stained with either phosphotungstic acid (pH 8.9) or silicotungstic acid (pH 7.0). The fibrils from the different species were found to be of similar width (10.5 to 12.5 nm) with the exception of the lapine samples...

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Collagen type IX from human cartilage: a structural profile of intermolecular cross-linking sites.

Type IX collagen, a quantitatively minor collagenous component of cartilage, is known to be associated with and covalently cross-linked to type II collagen fibrils in chick and bovine cartilage. Type IX collagen molecules have also been shown to form covalent cross-links with each other in bovine cartilage. In the present study we demonstrate by structural analysis and location of cross-linking...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1991

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)67713-6