C. Granier

Enzymatic transfer of oligosaccharide from oligosaccharide-lipids to an Asn-Ala-Thr containing heptapeptide.

Abstract Thyroid rough microsomes catalyzed the transfer of oligosaccharide from previously labeled thyroid [Man- 14 C] oligosaccharide-lipids to a synthetic dinitrophenylated heptapeptide containing a sequence Asn-Ala-Thr. The resulting product revealed an N-glycosidic attachment, probably to the asparaginyl residue in this sequence. The reaction which was time-dependent up to 1 h and exhibited an apparent Km of 94 μM for the DNP-heptapeptide was favoured by dimethylsul-foxide and inhibited by EDTA.

Preparation and partial characterization of polyclonal antibodies raised against a preselected sequence of calcium dependent lectins.

The synthetic-peptide strategy was used to generate antibodies raised against calcium-dependent lectins of vertebrates. We demonstrate that a synthetic peptide predicted from the amino acid sequence of the carbohydrate recognition domain can induce blocking antibodies which would react with, or in close vicinity of, the binding site of the parent molecule. As the preselected sequence was chosen in a consensus sequence region, we also present preliminary investigations of the use of specific antisera as a common biological probe against calcium dependent lectins. The availability of monospecific polyclonal sera opens new possibilities in biochemical and structural studies as well as immunodection of calcium dependent lectins.