Occurrence, Isolation, and Structures

Freeze-etching and small angle AT-ray data indicate that there are at least four, and probably as many as seven, bands of glycosaminoglycan along the axis of rat tail collagen, with four of the most prominent bands circumscribing the collagen fibrils.  

spectra of monomers and dimers of glycosaminoglycans have been recorded in solutions of ( H ldimethyl sulphoxide the NH- and OH-resonances were partially assigned.The temperature-dependence of the spectra suggests hydrogen bonding to the solvent with the exception of the C-4 

Lohmander, K. Madsen, and A. Hinek, Arch. Biochem. Biophys., 1979, 192, 148. 

Digestion of equine gastric mucosa with proteolytic enzymes releases hyaluronic acid, chondroitin 4- and 6-sulphate, and dermatan sulphate. This pattern of glycosaminoglycans differs from that found in pig mucosa, which contains heparin, dermatan sulphate, and chondroitin 4-sulphate, and in dog mucosa which contains hyaluronic acid and dermatan sulphate. 

Two proteoglycan-hyaluronate complexes have been isolated from bovine aorta under conditions of minimal proteolytic degradation. Both complexes 

Juvani, C. Friman, H. Ranta, and O. Wegelius, Biochim. Biophys. Acta, 1975, 411, 1. 

Hyaluronic acid of molecular weight 2 5 x 10 represents approximately 20% (w/w) of the hexuronic acids contained in the organic matter of chicken-egg shells.  

The isolation and the fractionation of urinary glycosaminoglycans have been achieved by partitioning complexes of the glycosaminoglycans and quaternary ammonium salts between a two-phase system of butan-l-ol and aqueous salt 

Rahemtulla, N.-G. Hoglund, and . Lovtrup, Comp. Biochem. Physiol., 1976, 53B, 295. 

The amino-acid composition of the link protein (mol. wt. 4 x 10 ) from swarm rat chondrosarcoma differs from that of the core protein.  

Occurrence, Isolation, and Structure.—Acid glycosaminoglycans in human platelets and leucocytes have been identified by using chondroitinase and Streptomyces hyaluronidase. The principal components are the chondroitin sulphates, with smaller amounts of hyaluronic acid, whereas heparan sulphate occurs only in leucocytes, possibly as a membrane component. Normal human kidney contains mainly hyaluronic acid and dermatan sulphate, with smaller proportions of chondroitin 4- and 6-sulphates and an over-sulphated chondroitin sulphate. A family of high-molecular-weight chondroitin sulphates possessing different degrees of sulphation has been identified in the nuclei of cultured mouse melanoma cells a minor component appears to be heparan sulphate.  

A method for preparing tritium-labelled oligosaccharides of hyaluronic acid has used the Wilzbach recoil technique the tritiated oligosaccharides are of potential use in studies of the mechanism of hyaluronidases. A four-fold helical form of hyaluronic acid has been detected using the data from fibre- 

A -Deacetylation occurred when keratan sulphate was treated with dilute sodium hydroxide, but the glycosylamine linkage of corneal proteoglycan was shown to be stable to 1.5M-sodium hydroxide in the presence of sodium boro-hydride at 80—83 °C.  

D-GalNAcp-[(L-IdUA/7-D-GalAAcp), -(L-IdUA/ -D-GaliVAcp) -(D-GlcUAp- 

The proteoglycan isolated from normal human intervertebral discs consists of chains of chondroitin sulphate and keratan sulphate, having molecular weights in the region of 2 x 10 and 1 x 10 , respectively, attached to a common peptide core. Neither chondroitin 4-sulphate nor hyaluronic acid was detected, although both have been reported to be present in the disc. 

Kjems and K. Lebech, Acta Pathol. Microbiol. Scand., 1976, 84B, 162. 

Desulphated keratan sulphate has been shown to interact with wheat-germ agglutinin, supporting the view that non-consecutive (1 - 4)-2-acetamido-2-deoxy-j8-D-glucopyranosyl residues interact specifically with the lectin to precipitate the complex. The distribution and chemical composition of keratan sulphate in various tissues, including those from a patient with Marfan syndrome, have been related to ageing. 

Nearest-neighbour analysis has been used to determine the sequences of heparin and heparan sulphates. Structures have been proposed for heparan sulphates A, B, and D based on analysis of the products released by the actions of heparinitase and heparinase from Flavobacterium heparinum.  

Rosenberg, C. Wolfenstein-Todel, R. Margolis, S. Pal, and W. Strider, /. Biol. Chem., 

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