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Open AccessJournal ArticleDOI

Isolation and characterization of proteoglycans from the swarm rat chondrosarcoma.

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TLDR
Proteoglycan monomer (D1) and aggregate (A1) preparations were isolated from 4 M guanidinium chloride extracts of the Swarm rat chondrosarcoma and contained only small proteoglycan fragments, indicating that extensive enzymatic degradation had occurred.
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This article is published in Journal of Biological Chemistry.The article was published on 1975-08-10 and is currently open access. It has received 543 citations till now. The article focuses on the topics: Proteoglycan & Benzamidine.

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Citations
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Journal ArticleDOI

A murine tumor producing a matrix of basement membrane

TL;DR: A murine tumor previously classified as a poorly differentiated chondrosarcoma is studied, and it is shown at the ultrastructural level that the tumor matrix is a homogeneous, nonfibrillar material, resembling basement membrane.
Journal ArticleDOI

Culture and growth characteristics of chondrocytes encapsulated in alginate beads.

TL;DR: Preliminary studies with collagen and chitosan matrixes encapsulated in "hollow" beads suggest that cell growth and morphology are profoundly influenced by the composition of the cellular environment.
Journal ArticleDOI

Isolation and characterization of two sialoproteins present only in bone calcified matrix.

A Franzén, +1 more
- 15 Dec 1985 - 
TL;DR: Antigenicity of sialoprotein II was not affected by reduction and alkylation, was only partially lost upon trypsin digestion and was completely lost upon fragmentation of the core protein by alkaline-borohydride treatment, indicating that all antigenic sites were located in the protein portion.
Book ChapterDOI

Structure and Metabolism of Connective Tissue Proteoglycans

TL;DR: The segregation of the proteoglycans into a separate category is based on a few specific characteristics, including the fact that the d-glucuronic-acid-containing repeating disaccharide of chondroitin, N-acetylchondrosine, has recently been identified as a component of thyroglobulin.
Journal ArticleDOI

Identification of a monoclonal antibody that specifically recognizes corneal and skeletal keratan sulfate. Monoclonal antibodies to cartilage proteoglycan

TL;DR: The 1/20/5-D-4 monoclonal antibody appears to recognize a common determinant in their polysaccharide moieties, consistent with several biochemical analyses showing the absence of keratan sulfate in proteoglycan synthesised by this tissue.
References
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Journal ArticleDOI

The Sialic Acids XI. A PERIODATE-RESORCINOL METHOD FOR THE QUANTITATIVE ESTIMATION OF FREE SIALIC ACIDS AND THEIR GLYCOSIDES

TL;DR: The periodate-resorcinol method was substantially more sensitive than the resorcinl procedure, was not affected by lipids, amino acids, or sugars, and could be used to detect free or glycosidically bound sialic acids on paper chromatograms.
Book

Chemistry and molecular biology of the intercellular matrix

TL;DR: This book will not become a unity of the way for you to get amazing benefits at all, but, it will serve something that will let you get the best time and moment to spend for reading the book.
Journal ArticleDOI

The specific interaction of hyaluronic acid with cartilage proteoglycans

TL;DR: The addition of small amounts of hyaluronic acid to disaggregated cartilage proteoglyans produced a large increase in hydrodynamic size on gel chromatography and there was no such interaction when proteoglycans were mixed with other polyanions in comparable proportions.
Journal ArticleDOI

Proteinpolysaccharide Complex from Bovine Nasal Cartilage A COMPARISON OF LOW AND HIGH SHEAR EXTRACTION PROCEDURES

TL;DR: Two procedures for isolating 80 to 85% of the total hexuronic acid from bovine nasal cartilage as proteinpolysaccharide complex are described and compared, and it is suggested that disaggregation is fundamental to the extraction process.
Journal ArticleDOI

Proteinpolysaccharide complex from bovine nasal cartilage. The function of glycoprotein in the formation of aggregates.

TL;DR: Reduction and alkylation of isolated proteoglycan subunit and of the glycoprotein fraction suggest that disulfide bonds in both are required for aggregation, but that those in the former are more sensitive to reduction.
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