-transparent.png){kind=logo}
Transglycosylation reactions of alpha-amylases from human pancreatic juice and saliva were examined by using O-6-deoxy-6-[(2-pyridyl)amino]-alpha-D-glucopyranosyl-(1 leads to 4)-O-alpha-D-glucopyranosyl-(1 leads to 4)-O-alpha-D-glucopyranosyl-(1 leads to 4)-O-alpha-D-glucopyranosyl-(1 leads to 4)-D-glucopyranose as a substrate and O-alpha-D-glucopyranosyl-(1 leads to 4)-O-alpha-D-glucopyranosyl-(1 leads to 4)-1-deoxy-1-[(2-pyridyl)amino]-D-glucitol as an acceptor. The transfer reaction was estimated by quantitation of O-alpha-D-glucopyranosyl-(1 leads to 4)-1-deoxy-1-[(2-pyridyl)amino]-D-glucitol produced by the enzymes from the transfer products, because the acceptor was not hydrolyzed. The amount of O-alpha-D-glucopyranosyl-(1 leads to 4)-1-deoxy-1-[(2-pyridyl)amino]-D-glucitol in the digest with pancreatic alpha-amylase was six times that in the digest with salivary alpha-amylase at the stage when the substrate was completely consumed, and the difference increased gradually on further incubation. The phenomenon can be applied to differentiate the two alpha-amylases in human serum.
K Omichi, and
T Ikenaka
September 1981,
Biochimica et biophysica acta,
K Omichi, and
T Ikenaka
November 1970,
The American journal of digestive diseases,
K Omichi, and
T Ikenaka
March 1984,
Clinica chimica acta; international journal of clinical chemistry,
K Omichi, and
T Ikenaka
May 1984,
Gene,
K Omichi, and
T Ikenaka
October 1979,
Clinica chimica acta; international journal of clinical chemistry,
K Omichi, and
T Ikenaka
December 1964,
Experimental cell research,
K Omichi, and
T Ikenaka
December 2003,
Organic letters,
K Omichi, and
T Ikenaka
October 1967,
Archives of biochemistry and biophysics,
K Omichi, and
T Ikenaka
April 1981,
Biochimica et biophysica acta,
