Abstract
The nature of the carbohydrate-peptide bond and the composition of the carbohydrate chain in a β-1,3-glucanase from the marine molluskS. sachalinensis has been investigated. According to the results of the phenol-sulfuric acid method, the neutral sugars amounted to 6.5% of the molecular weight of the enzyme. The composition of the neutral sugars (Glc : Gal : Man 5:2:1) was determined by the GLC method. It was shown that the β-1,3-glucanase molecule contains no uronic or sialic acids. The amount of amino sugars (15% with equal amounts of glucosamine and galactosamine) was established by amino acid analysis. Alkaline degradation led via the β-elimination reaction to the splitting out of 50% of the neutral sugars and showed the existence of an O-glycosidic bond in the enzyme molecule. Various actions on the carbohydrate moiety (periodate oxidation and treatment with glycosidases) caused no appreciable change in the hydrolyzing capacity of the enzyme.
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Pacific Ocean Institute of Bioorganic Chemistry, Far Eastern Scientific Center, Academy of Sciences of the USSR, Vladivostok. Translated from Khimiya Prirodnykh Soedinenii, No. 3, pp. 286–291, May–June, 1982.
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Myastovskaya, O.M., Sova, V.V. & Elyakova, L.A. Characteristics of a β-1,3-glucanase fromSpisula sachalinensis as a glycoprotein. Chem Nat Compd 18, 261–267 (1982). https://doi.org/10.1007/BF00580447
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DOI: https://doi.org/10.1007/BF00580447