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Assessing the Secretory Capacity of Pancreatic Acinar Cells
Published on: August 28, 2014
Optimum pH control mechanism for porcine pancreatic alpha-amylase
K Ishikawa1, I Matsui, K Honda
1National Institute of Bioscience and Human Technology, Ibaraki, Japan.
Bioscience, Biotechnology, and Biochemistry
|June 1, 1995
Abstract:
We studied the substrate-dependence of pH activity of porcine pancreatic alpha-amylase by using a series of p-nitrophenyl maltooligosaccharides. The mechanism controlling the optimum pH of mammalian alpha-amylase involved the reception and recognition of a substrate component at some other substrate binding sites, in addition to those at subsite 5 that were reported previously [K. Ishikawa et al., Biochemistry, 32, 6259-6265 (1993)].
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