ENZYMATIC TRANSGLYCOSYLATION AS A MEANS O F BETA-1,3-1,6-GLUCOOLIGOSACCHARIDE DETECTION AND IDENTIFICATION IN LAMINARIOLIGOSACCHARIDE MIXTURES

A homologous series of p-nitrophenyllaminarioligosides (1G(n)Np) and p -nitrophenylgentiooligosides (gG(n)Np) were analyzed by HPLC, and thei r retention time logarithms (log tau) were plotted against the degree of polymerization (d.p.). This gave straight lines for both series, wi th the slope for gG(n)Np being considerably steeper than that for 1G(n )Np. For p-nitrophenylglycosides of the oligosaccharides with mixed be ta-1,3;1,6-structure, the analogous plot lies between the above-mentio ned lines. On the basis of these facts, a method of qualitative detect ion and semiquantitative determination of beta-1,3;1,6-glucooligosacch arides is proposed, involving the latter as donor components in a tran sglycosylation reaction with the GNP acceptor catalyzed by the endo-be ta-1,3-glucanase LIV. The formed products are subsequently analyzed by HPLC. As an example, identification of components was carried out in mixtures of beta-1,3;1,6-glucotri- and tetramers obtained by digestion of laminaran with different endo-beta-1,3-glucanases. A mixture of tr isaccharides was shown to contain mainly [GRAPHICS] [GRAPHICS] level p re-coiled bodies have a compact fibrillar structure, whereas coiled bo dies resemble a tangle of coiled threads. Although both pre-coiled bod ies and coiled bodies contain the nucleolar protein fibrillarin, the a ssembly of coiled bodies is separated both in time and in space from r ibosome synthesis, Our results suggest that the embryonic 'nucleolus-l ike body' is a structural scaffold that nucleates independently the fo rmation of the coiled body and the assembly of the machinery responsib le for ribosome biosynthesis.