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- W1992482494 abstract "The solubility of the orthorhombic polymorph A of α-amylase was determined at pH = 8 in KSCN, KCl, K2SO4 and NaCl solutions and at pH = 7, 8 and 9 in NaCl solutions. The effectiveness of anions in decreasing the solubility of α-amylase at pH = 8 is SO2−4>Cl−>SCN−. This order is in agreement with the Hofmeister series. The decrease of pH towards the pI caused the solubility to decrease. Molecular interactions were studied by Quasi Elastic Light Scattering and Small Angle X-ray Scattering. For BPTI in NaCl solutions, the interactions change from repulsive to attractive once NaCl concentration is higher than 1M. For α-amylase (ionic strength 28 mM) interactions are slightly repulsive. However, under both conditions the macromolecules crystallize. The molecular interactions probably explain why the growth rate of BPTI is larger than that of α-amylase." @default.
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- W1992482494 date "1996-10-01" @default.
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- W1992482494 title "Prenucleation, crystal growth and polymorphism of some proteins" @default.
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- W1992482494 doi "https://doi.org/10.1016/0022-0248(96)00373-9" @default.
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