Some properties and the structure of a glucosamine-aspartic fragment from ovalbumin

Glycopeptides from Ovalbumin. Preparation, Properties, and Partial Hydrolysis of the Asparaginyl Carbohydrate*

“…T A he initial studies of ovalbumin concerning the structure of the carbohydrate moiety have centered around an analysis of the composition of the carbohydrate, the preparation of simple glycopeptide fragments, and the reactions which might indicate the nature of the protein-carbohydrate linkage (Jevons, 1958;Nuenke and Cunningham, 1961;Bogdanov et al, 1962Bogdanov et al, , 1964; Lee and Montgomery. 1962;Clamp and Hough, 1963;Marks et al, 1962Marks et al, , 1963Micheel et al, 1963;Yamashina et al, 1963;Tsukamoto et al, 1964).…”

“…This paper describes the digestion of ovalbumin with pronase, a crystalline protease from Streptomyces griseus that has been applied previously to ovalbumin (Bogdanov et al, 1964;Fletcher et al, 1963a,b;Yamashina and Makino, 1962). Peptides were obtained that differ only in their amino acid composition.…”

Binding of methylmercury to ovalbumin as methylmercuric cysteine

“…Enzymic digestion with Pronase was employed instead of acid hydrolysis to reduce the potential loss of ^Hg. Pronase, a protease from S. griseus, has been used successfully for the digestion of ovalbumin (Bogdanov et al, 1964; Narita and Ishii, 1962; Yamashina and Mikuno, 1962).…”

Attachment site of carbohydrate in a mouse immunoglobulin light chain

“…In those cases it was shown that the carbohydratepeptide bond links Ci of the sugar to C3 of aspartic acid or asparagine. This might occur either by linking the /3-carboxyl group of aspartic acid to the 1-aminogroup of 2-deoxy-2-acetamidoglucosylamine, or by 946 linking asparagine through its /3-amido group to the 1-hydroxyl group of 2-deoxy-2-acetamidoglucose (Marks et al, 1963;Yamashina et al, 1963;Tsukamoto et al, 1964;Bogdanov et al, 1964). It seems more likely to go via the latter pathway, i.e., via UDP-jYacetylglucosamine to asparagine.…”