CARRAGEENANS function in the intercellular regions of certain red seaweeds1–3 and have residues of two types, designated A (α-linked) and B (β-linked), which are arranged alternately and may themselves occur as different variants. When A is 3,6-anhydro-D-galactose 2-sulphate and B is D-galactose 4-sulphate, the structure is an idealization known as ι-carrageenan4. Another member of the family, ϰ-carrageenan, has the same structure except that the 2-positions carry little or no sulphate. Native polysaccharides usually depart from these idealizations in having a proportion of A residues in the form of 6-sulphate (I)5,6. Evidence from X-ray diffraction7 and optical rotation4,8,9 indicates that the gel framework is formed by cross-linking of chains in double helices, and that the 6-sulphate residues must represent8 impediments to this process, or “kinks” in the helix strand; schematically, the chain is IV rather than III. It is tempting to propose that these kinks are used to regulate the extent of helix formation, and therefore the physical and biological properties7. We report here a search for an enzyme which would be involved in such control.
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LAWSON, C., REES, D. An Enzyme for the Metabolic Control of Polysaccharide Conformation and Function. Nature 227, 392–393 (1970). https://doi.org/10.1038/227392a0
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