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Growth inhibition of lysozyme crystals at high hydrostatic pressure
Author(s) -
Groß Michael,
Jaenicke Rainer
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80768-x
Subject(s) - lysozyme , hydrostatic pressure , chemistry , biophysics , protein crystallization , hydrostatic equilibrium , high pressure , biochemistry , biology , mechanics , crystallization , physics , organic chemistry , quantum mechanics
The influence of high hydrostatic pressures on the crystallization of hen egg‐white lysozyme has been determined by growing lysozyme crystals with a capillary technique adapted to high pressure conditions and monitoring the residual protein concentration remaining in the supernatant. Pressure is found to reduce the rate of crystallization and to enhance the solubility of lysozyme in 1 M NaCl, pH 4.66. The volume change calculated from the latter result amounts to 12.5 ml/mol. This value is too small to be detectable by comparison of total molar volumes.