Abstract
Abstract Heparin, dextran sulphate, dextran phosphate, chondroitin sulphate and degraded Λ-carrageenan inhibit peptic activity by substrate occlusion or depletion. This holds for various substrates and enzyme preparations, but the amount of inhibition observed varies with method and inhibitor used. The most active inhibitors of the series are disulphated on at least alternate sugar residues and in addition to disulphation high molecular weight confers, in certain conditions, greatest activity. High and low molecular weight macroanions have different inhibition characteristics and it is concluded that activity may depend upon the structure of the substrate-inhibitor complexes formed. Inhibition is not observed when substrate-inhibitor interaction does not occur, as when pepsin or N-acetyl-L-phenylalanine-L-diiodotyrosine (APDT) are used as substrate.
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