Abstract: An affinity chromatography method for the separation and pruification of two active forms of urokinase from a crude urokinase preparation. The method employs an extracting agent of agmatine covalently coupled to the surface of a water-insoluble solid support material such as agarose, and three separate specific buffer solutions. A low ionic strength buffer, such as 0.01 molar sodium phosphate buffer, pH 6.0-9.0, is used in preparing the loading solution and for washing the extracting agent. A slightly higher ionic strength buffer, such as 0.02 molar sodium phosphate buffer, pH 6.0-9.0, is used as a first eluant for eluting from the extracting agent a first active form of urokinase which is characterized by a molecular weight of approximately 33,400 and a specific activity of approximately 226,000 CTA units/mg protein. A still higher ionic strength buffer with added salt, such as 0.1 molar sodium phosphate -- 0.4 molar sodium chloride buffer, pH 5.0-8.

Abstract: Lysozyme from human, avian, non-human mammalian, and vegatable sources is isolated from said sources and provided in a high degree of purity by adsorbing the lysozyme upon chitin obtained from Loligo vulgaris by contacting said chitin with an acidic aqueous suspension of the crude lysozyme containing material, and eluting the pure lysozyme from said chitin with aqueous acid.