Comparison of individual genomes;
Consensus and multiple sequence alignment;
Multiple mapping of genome to contigs;
Multiple mapping of contigs to contigs;
Consensus mapping to contigs.
P-xylosidase (EC 22.214.171.124) is an enzyme that catalyses the hydrolysis of 4-O-beta-D-xylosyl-(1–>4)-alpha-D-galactosides from p-nitrophenyl 4-O-beta-D-xylopyranosyl-(1–>4)-alpha-D-galactopyranoside (Kushiro et al. 1985). The kinetic parameters of p-nitrophenyl xylosides as substrates for P-xylosidase were determined (Kushiro et al. 1985).
The screening for new xylanase in marine actinomycetes was undertaken on a basal agar medium containing 1% beechwood xylan, and was found that the production of xylanases on this medium is variable. Among the 101 tested actinomycetes, only a few have proven to be xylanase producers, i.e. AS3.1184, AS3.1210, AS3.1308, AS3.1409, AS3.1412, and AS3.1501.
These materials may be used to produce the antigen necessary for development of an enzyme immunoassay (EIA) for recombinant human xylosidase-A.
Tests for Endogenous Oligosaccharides
The glycoproteins, which are abundant in the blood plasma, are always present in a partially modified form. The most abundant modified forms found in humans are the glycans attached to the serum proteins in the plasma. The galactose and N-acetylglucosamine residues in these glycans are linked to the serine and threonine residues of serum proteins via one or more N-acetyl-D-glucosamine or N-acetyl-D-galactosamine residues. A breakdown of the blood plasma glycoproteins can be detected by specific oligosaccharides.
For our study, we used these oligosaccharides as an indirect marker to assess the fragmentation of the blood plasma glycoproteins.
In this study, we used two complementary analytical techniques 70238732e0
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