English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

We measured UDP-GlcNAc:Gal (beta 1-4) Glc (or GlcNAc) (beta 1-3) N-acetylglucosaminyltransferase activities in bovine (Holstein and Jersey cow) and human colostrums, and found in human colostrums sufficient activity to study the enzyme properties while not in bovine colostrums. The properties (requirements, pH optimum, acceptor specificity and Km values for lactose and N-acetyllactosamine) of the enzyme from human colostrum were very similar to those from human serum and urine. The reaction product was hydrolyzed by beta-N-acetylhexosaminidase, indicating that the N-acetylglucosaminyl residue was beta-linked to lactose. Methylation and hydrolysis of the reaction product from lactose [3H] labeled at the terminal galactose yielded 2, 4, 6-tri-O-methyl [3H] galactose. Thus the structure of the product was demonstrated to be GlcNAc (beta 1-3) Gal (beta 1-4) Glc (lacto-N-triose II). On the other hand, bovine sera contained N-acetylglucosaminyltransferase catalyzing the transfer of N-acetylglucosamine from UDP-GlcNAc to lactose. The enzyme activities were approximately 1/6-1/4 of that contained in human serum. The presence of (beta 1-3) N-acetylglucosaminyltransferase in human colostrum and its absence in bovine colostrums, apparently corresponds with the presence and absence of oligosaccharides containing lacto-N-triose II structure in colostrum.

nihon juigaku zasshi/japanese journal of veterinary science

The relationship between the (.BETA.1-3)N-acetylglucosaminyltransferase and the presence of oligosaccharides containing lacto-N-triose II structure in bovine and human milk.