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Relative effectiveness of various anions on the solubility of acidic Hypoderma lineatum collagenase at pH 7.2
Author(s) -
Carbonnaux Claire,
RiesKautt Madeleine,
Ducruix Arnaud
Publication year - 1995
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560041018
Subject(s) - solubility , chemistry , crystallization , hofmeister series , ammonium sulfate , ammonium , inorganic chemistry , salt (chemistry) , chromatography , organic chemistry
The effects of various anions on decreasing the solubility of acidic Hypoderma lineatum collagenase at pH 7.2 and 18 °C were qualitatively defined by replacing the crystallizing agent of known crystallization conditions by various ammonium salts. The solubility curves measured in the presence of the sulfate, phosphate, citrate, and chloride ammonium salts gave the following ranking of anions: HPO 4 2‐ /H 2 PO 4 − > SO 4 2‐ > citrate 3‐ /citrate 2‐ >> Cl − . This order is in agreement with the Hofmeister series. In a previous study on the solubility at pH 4.5 of lysozyme, a basic protein, the effectiveness of anions in decreasing the solubility was found to be in the reverse order. This suggests that the effectiveness of anions in the crystallization of proteins is dependent on the net charge of the protein, i.e., depending on whether a basic protein is crystallized at acidic pH or an acidic protein at basic pH.