The Editor8 of the Biochemical Journal accept no re.spon8ibility for the Report8 of the Proceeding8 of the Society. Ab8tract8 of papers read are publi8hed as received from the author8.] PROCEEDINGS OF THE BIOCHEMICAL SOCIETY The 352nd Meeting of the Biochemical Society was a joint meeting with the Scandinavian Biochemical Societies and was held in the Department of Biochemi8try of the Univer8ity of Cambridge on Thur8day, Friday and Saturday, 28-30 June 1956, 8tarting at 2 p.m. on Thur8day 28 June. The following papers were read: COMMUNICATIONS Cholinesterases in Bovine Plasma. By D. C. HARDWICK. (In8titUte of Animal Phy8iology, Babraham, CJambridge8hire) Crude albumin, separated from bovine plasma by the ether technique of Kekwick & Mackay (1954), was found to destroy acetylcholine. As bovine plasma had previously been reported to contain negligible amounts of cholinesterases (Augustinsson, 1948), the cause was further investigated. Using the Warburg technique, bovine plasma was found to hydrolyse acetylcholine and also butyrylcholine. Some separation of the activities into the globulin impurities of the crude albumin could be achieved as Kekwick, Mackay & Martin (1953) had found to be the case for human plasma cholinesterase. This material hydrolysed acetylcholine and butyrylcholine at approximately equal rates. Acetyl ,-methylcholine was attacked at a lower rate and so were triacetin and tributyrin. Benzoylcholine was not attacked. 80-90 % of the choline ester and triacetin hydrolysis was inhibited by 10-5M eserine, but only 30-40 % of the activity against tributyrin was inhibited; DFP at 10-6M inhibited butyrylcholine hydrolysis; 284C 51 (Fulton & Mogey, 1954) at 10-6m inhibited acetylcholine hydrolysis to about 70 %. The results suggested the presence of a 'true' (acetyl) cholinesterase and a butyryl cholinesterase; additive experiments with both substrates present failed, since butyrylcholine inhibits true cholinesterase (Cohen, Warringa & Bovens, 1951). A crude separation of the two enzymes has been achieved by ammonium sulphate precipitation. Recently, Bannister, Whittaker & Wijesundra (1953) found ox spleen to contain a butyryl cholinesterase and Mendel & Myers (1955) found much of this activity was eserine-sensitive. On the basis of inhibition by selective inhibitors the latter authors define this enzyme as a pseudocholinesterase. The butyryl cholinesterase described here may therefore qualify as a 'pseudo' cholinesterase, though it would not be so classified by the earlier definition (Mendel, Mundell & Rudney, 1943) that pseudocholinesterases hydrolyse benzoylcholine. The redefinition indicates the unsatisfactory nature of this nomenclature.