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Production by normal human erythrocytes of a substrate for cholinesterase has been demonstrated. At body temperature, the formation and hydrolysis of the cholinesterase substrate is delicately controlled. At lowered temperatures, 0 to -1.5 C., production of cholinesterase substrate greatly exceeds its hydrolysis. The quantity of cholinesterase substrate capable of exerting its influence governs the quantity of dextrose converted to lactic acid by the erythrocyte under anaerobic conditions. The observations corroborate and extend the suggestion of Lindvig, Greig, and Peterson that cholinesterase is part of a cellular system governing erythrocyte permeability. The balance between production and hydrolysis of cholinesterase substrate at low temperature exhibits the same undulating fluctuations during red cell storage that have been noted for other erythrocyte metabolic functions.

The fluctuating capacity of stored erythrocytes to release gas when suspended in the presence of dextrose in Krebs-Ringer bicarbonate solution in an atmosphere of 5 per cent CO2-95 per cent N2 is demonstrated. A not dissimilar fluctuation of the cholinesterase activity of the stored cells is reported. Possible seasonal variation in the state of red cells is suggested. Some implications of these observations for erythrocyte storage are suggested.

It is possible to prepare self-stabilizing solutions of hemoglobin from human erythrocytes by the use of dextrose, nicotinic acid amide and ammonia during the preparation and in the final solutions themselves. Co++, Mn++ and Mg++ ions, nile blue and hexose diphosphate contribute to the speed of stabilization of these solutions. Stabilization is obtained by the faculty of the solutions, presumably by enzymic action, to convert the hemoglobin to the reduced form and to maintain it in this form. The hemoglobin solutions described are suitable for intravenous administration.

Reports on the efficacy of gamma globulin (immune serum globulin) prepared from normal adult human serum in the prevention of homologous serum hepatitis (viral hepatitis B), while indicating some prolongation of incubation period1 or some degree of protection against the disease in battle casualties who have been given transfusions,2 have provided evidence that this material is considerably less potent in prophylaxis against this disease than against infectious (epidemic) hepatitis (viral hepatitis A). In addition, a previous attempt1b to neutralize homologous serum hepatitis virus in icterogenic serum with 20 ml. of normal gamma globulin was unsuccessful. In view of the frequency and importance of the problem of homologous serum hepatitis, effective prophylactic measures would be of great value in making the administration of blood or blood products safer. Since there does not exist at present a satisfactory method for inactivation of hepatitis virus in these materials before injection,

Ninety-four units of blood have been collected, glycerolized, stored in the frozen state at either —80 C or —120 C, deglycerolized, stored at 4 C, and then used clinically. A technique has been developed for maintaining sterility at every step. Even after storage at very low temperatures for periods up to 19 months, the red blood cells appeared therapeutically comparable to cells stored at 4 C up to 21 days in a standard A.C.D. (anticoagulant acid citrate dextrose) solution. The longevity of red blood cells in the circulatory system of the recipient was studied by using chromium 51 for labeling and was found to be independent of the duration of storage. The loss of red blood cells by lysis during the process as a whole seemed to be due entirely to irreversible random damage during collection and handling rather than to storage at low temperature. The sterility of the system made possible an additional postthawing storage of the red blood cells for up to 11 days at 4 C before use in transfusions. No transfusion reactions of any kind were noted.

As early as 1947, Polge, Smith, and others1-3 showed that tissues exposed to glycerol and other polyhydric alcohol subsequently could be frozen and thawed without significant harm. The implication of this observation to blood banking was readily apparent, but practical considerations prevented its immediate translation to methods of red cell preservation. This was chiefly because glycerol must be removed from the red cells before transfusion.The Cohn fractionator, developed in 1951, for the separation of blood into its component parts4 was found to possess certain features which made it uniquely applicable to the glycerol processing of red cells prior or subsequent to preservation in the frozen state. This Cohn-ADL fractionator contains a sterile centrifuge that operates at fixed temperatures with no limitations on the volume of solutions that may be perfused through the cellular mass revolving inside the centrifuge bowl.5Preliminary studies with this apparatus by Tullis

From previous collaborative studies with the Worcester State and Medfield State Hospitals and the Protein Foundation, we have reported evidence for a taraxein-like substance found in human plasma proteins which may be related to schizophrenia.1,2 The plasma factor has been shown to disturb the performance of trained rat behavior to a significantly greater degree when derived from the blood of schizophrenic patients than from the blood of psychotic nonschizophrenic individuals or from normal persons. The factor may be a concomitant of disease or stress processes so plasma factor titers were investigated in physically ill persons without psychiatric disorders to settle this point. METHODS Nonpsychotic donors for the study were patients of the Rutland Heights VA Hospital selected from the following categories: (1) tuberculosis, (2) carcinoma, (3) chronic hospitalization, and (4) post-operative. Collections from psychotic individuals were obtained at the Medfield and Worcester State Hospitals primarily