filtration on sephacryl s 200 hr the column 1 6 u00d7 69 6 cm coupled to a fplc system was operated with a flowthrough rate of 1 ml minute and 0 1 ml of the enzyme which was glycerinated and purified by means of salting out chromatography served as specimen after a twofold dilution the following served as reference proteins cytochrom c horse myoglobin whale myoglobin horse aldolase rabbit muscle carboanhydrase and bovine serum albumin the molecular weight of the acylase is 65 000 u00b1 5000 a molecular weight of 55 000 u00b1 4000 was determined in gel electrophoresis in the presence of sodium dodecylsulfate sds for the denatured enzyme accordingly the acylase consists of a polypeptide chain of an unusual length the following were used for the calibration curve u03b1 2 macroglobulin equine plasma phosphorylase b rabbit muscle glutamate dehydrogenase bovine liver lactate dehydrogenase swine muscle and trypsin inhibitor soy bean a dependency of the acylase activity on the concentration of various n acetyldehydroamino acids the activity of the acylase was determined under standard conditions cf example 8a with various n acetyldehydroamino acids in concentrations of 0 1 to 300 mm a second series of measurements with n acetyldehydroleucine in the above indicated concentration range was placed in 0 1m tris phosphoric acid buffer the k m value for adl is 4 5 mm in glycine buffer the kinetic data for the splitting of the acetyldehydroamino acids is collated in table 9 table 9______________________________________kinetic data of n acetyldehydroleucine.