Characterization of a NovelN-Acetylneuraminate Lyase from Staphylococcus carnosus TM300 and Its Application toN-Acetylneuraminic Acid Production

2012 ◽  
Vol 60 (30) ◽  
pp. 7450-7456 ◽  
Author(s):  
María Inmaculada García García ◽  
Agustín Sola Carvajal ◽  
Francisco García Carmona ◽  
Álvaro Sánchez Ferrer
1968 ◽  
Vol 46 (8) ◽  
pp. 983-988 ◽  
Author(s):  
J. Z. Augustyniak ◽  
W. G. Martin

Two glycopeptides (A and B) were isolated from pronase-digested vitellenin, the protein moiety of the low-density lipoprotein of hen's egg yolk. Aspartic acid was the only N-terminal amino acid of both glycopeptides but only A contained N-acetylneuraminic acid. A contained 55% hexose (mannose), 14% hexosamine, 12% N-acetylneuraminic acid, 0.71% amide nitrogen, and its molecular weight was 2.3 × 103. The corresponding values for B were 64, 17, 0.0, 0.75, and 2.0 × 103. Chemical analyses showed that B (and probably A) occurs in vitellenin with the heteropolysaccharide group bound N-glycosidically via the β-amide group of an asparaginyl residue. The indicated structure is R∙(NH)Asp∙Thr∙Ser∙(Ala, Gly, Val)∙Ile, where R, the heteropolysaccharide group, contains 2 hexosamine and 8 hexose residues.


Gene ◽  
1990 ◽  
Vol 94 (1) ◽  
pp. 37-43 ◽  
Author(s):  
Stefan Seeber ◽  
Christoph Kessler ◽  
Friedrich Götz

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