Clinica chimica acta; international journal of clinical chemistry, 244(2), 145-154 (1996-01-31)
The method of assay of neutral alpha-glucosidase from human kidney and urine using beta-maltosides (p-nitrophenyl-beta-D-maltoside [NP-beta-D-maltoside], 2-chloro-4-nitrophenyl-beta-D-maltoside]) [CNP-beta-D-maltoside] and 4-methylumbelliferyl-beta-D-maltosides ([MU-beta-D-maltoside]) as substrates and beta-glucosidase as an auxiliary enzyme is proposed. All three beta-maltosides are suitable substrates for the determination
Journal of biochemistry, 100(5), 1353-1358 (1986-11-01)
p-Nitrophenyl O-6-deoxy-6-[(2-pyridyl)amino]-alpha-D-glucopyranosyl-(1----4)-O-alpha- D-glucopyranosyl-(1----4)-O-alpha-D-glucopyranosyl-(1----4)-O-alpha-D- glucopyranosyl-(1----4)-alpha-D-glucopyranoside (FG5P) is hydrolyzed by human pancreatic a-amylase (HPA) or salivary alpha-amylase (HSA) to O-6-deoxy-6-[(2-pyridyl)amino]-alpha-D- glucopyranosyl-(1----4)-O-alpha-D-glucopyranosyl-(1----4)-D-glucose (FG3) and p-nitrophenyl alpha-maltoside or to O-6-deoxy-6-[(2-pyridyl)amino]-alpha-D-glucopyranosyl-(1----4)-O-alpha- D-glucopyranosyl-(1----4)-O-alpha-D-glucopyranosyl-(1----4)-D-glucose (FG4) and p-nitrophenyl alpha-glucoside. The use of alpha-D-glucosidase (maltase) [EC 3.2.1.20] of Saccharomyces
Archives of oral biology, 44(2), 119-127 (1999-04-17)
Human salivary alpha-amylase participates in the initial digestion of starch and may be involved in the colonization of viridans streptococci in the mouth. To elucidate the role of histidine residues located near the starch-binding site on the streptococcal-binding activity, the
Journal of biochemistry, 107(4), 546-549 (1990-04-01)
Human non-salivary, non-pancreatic alpha-amylase (yHXA) is the gene product of a newly found human alpha-amylase gene expressed in yeast. Its mode of action on a fluorogenic derivative of p-nitrophenyl alpha-maltopentaoside, FG5P (FG-G-G-G-G-P), was examined at various pH values to elucidate
Journal of bacteriology, 165(3), 918-922 (1986-03-01)
In wild-type Escherichia coli the activity of the maltose transport system is dependent on a periplasmic maltose-binding protein. It has been possible, however, to isolate mutants in which transport activity is mediated by the membrane components of the system and
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