Glycoproteins less-acidic

Edge ABS, Faltynek CR, Hof L, Reichert LE Jr, Weber P. Deglycosylation of glycoproteins by trifhioromethanesulfonic acid. Anal Biochem 1981 118 131-137. 

Gambacorti-Passerini C, Barni R, le Coutre P et al. Role of alphal acid glycoprotein in the in vivo resistance of human BCR-ABL(+) leukemic cells to the ABL inhibitor STI571. J Natl Cancer Inst 2000 92 1641-1650. 

The anisotropy A, at 20°C, of calcofluor free in solution increases from 0.1830 0.0007 to 0.1982 0.0007 and 0.2094 0.0014 in the presence of ai-acid glycoprotein and HSA, respectively. The increase in anisotropy indicates that the calcofluor interacts with both proteins (Le Tilly and Royer, 1993). 

Although an amidase, this enzyme is considered here partly because of its prob le importance in the degradation of hexosamine-containing glycoproteins, but also because the initial product of the enzymic reaction (l-amino-2-acetamido-l,2-dideoxy-0-i>-glucopyrano3e LXX, Ri = R2 = Rs = R< = H) is labile and liberates A -acetyl-i>-glucosamine and ammonia, under the mildly acidic conditions often employed for the a ay of the enzyme (Makino ei al., 1966 Conchie and Strachan, 1969). 

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