Structural characteristics of heparan sulfates with varying sulfate contents.

Structural properties of heparan sulfate preparations from hog mucosa and beef lung sources were obtained by application of Smith degradation and nitrous acid reactions. Products formed by these reactions indicated that most of the iduronic acid present in these mucopolysaccharides is ester sulfated, whereas N-sulfated glucosamine residues are ester sulfated much less frequently. Repeating units with sulfated iduronic acid found to occur almost entirely in single sequences.

Preparation of carcinoembryonic antigen (CEA) containing significantly increased amounts of galactose and galactosamine.

CEA was prepared by combined isoelectric precipitation, ultrafiltration and column chromatography under controlled conditions of pH. The resulting immunologically active materials were higher in carbohydrate (85-87%), N-acetyl galactosamine (10-11.5%) and galactose (28-32%) content than that previously reported.

The linkage of corneal keratan sulfate to protein.

The linkage of corneal keratan sulfate to protein has been investigated. After exhaustive digestion of bovine corneas with papain and pronase, a product was obtained in which aspartic acid was the predominant amino acid and constituted 59% of the total amino acids. A carbohydrate-protein linkage fragment was isolated from this preparation by a relatively simple procedure involving the following steps: (1) partial acid hydrolysis, adsorption of glycopeptides and other cationic material on Dowex 50-X2 (H+) and elution with 0.

The distribution of sulfated uronic acid and hexosamine residues in heparin and heparan sulfate.

Heparins from various sources and heparan sulfate from umbilical cords have been subjected to Smith-degradation and reaction with nitrites. These procedures were effective for providing data relating to the distribution of sulfated iduronic acid residues in the molecule. Results indicated that heparins may have, as a prominent structural feature of the molecule, non-sulfated uronic acid distributed in single sequences, much as had been shown previously for N-acetylglucosamine residues.