Abstract:
L-asparaginase is obtained in a highly purified, pyrogen free and stabilized form from a crude aqueous solution thereof, by adding to said solution an amino acid, such as glycine, adjusting the pH of the solution to from 7.0 to 9.2, preferably in the presence of a lower aliphatic alcohol, such as methanol, then heating the solution for a period of from 1 to 5 days at a temperature up to 65* C., preferably between 40* C. to 61* C., thereby denaturizing the inactive accompanying proteins without affecting the L-asparaginase. The precipitated, denatured proteins are then removed, as by centrifuge, the enzyme enriched solution then adjusted to a pH between 4.5 and 5.5 and fractionally precipitated with a 50 percent polyethylene glycol solution, the precipitate then washed with acetone and dried.
Abstract:
Foot-and-mouth disease virus solutions, used for the preparation of vaccines against the disease, are freed of undesirable protein contaminants accompanying the virus particles by subjecting the impure solution to fractional precipitation with polyethylene glycol solutions. The precipitate, containing the virus intigens is separated from the liquid phase which contains the proteins, preferably by centrifuging. The sediment consists of substantially purified virus antigen.
Abstract:
Fibrinolysokinase of good stability is isolated from culture solutions of actinomycetes by heat treatment at a low pH followed by fractional precipitation.
Abstract:
From a culture of E. coli the bacterial mass is flocculated by addition of an organic base or a salt thereof having an amino function and a molecular weight above 1,000. The flocculated cells are centrifuged, resuspended in water and precipitated by a water-miscible solvent, such as acetone. The cells which are simultaneously opened by the previous step are centrifuged away and again resuspended in water, whereby the enzyme is extracted from the cells. By addition of the organic base, mentioned above, to the suspension, the extracted cells, nucleic acids and ballast proteins are precipitated and are removed by centrifugation. The L-asparaginase is precipitated from the cell-free solution by addition of acetone.
Abstract:
L-asparaginase is obtained in concentrated purified form by fractional precipitation of an aqueous solution thereof with low molecular weight solvents, specifically diols of 4 to 8 carbon atoms, such as 2-methyl-pentane-diol-(2,4) and including such diols wherein one hydroxyl group is alkylated, for example 3methoxybutanol.
Abstract:
Crude L-asparaginase is freed of pyrogens by contacting solutions of the same containing weak buffers with diethylaminoethyl dextran gels. The process can be carried out according to batch techniques or in a continuous manner by using a chromatographic column.
Abstract:
ALKYLSULPHONYL-COBALAMINES ARE PRODUCED BY REACTING HYDROXO-COBALAMINE WITH ALKYL-SULPHINIC ACIDS AT AMBIENT TEMPERATURE OR AT SLIGHTLY ELEVATED TEMPERATURES. THEY MAY ALSO BE PREPARED BY REACTING CYANO-COBALAMINES WITH ALKYL-SULPHINIC ACIDS. THE ALKULSULPHONYLCOBALAMINES ARE USEFUL IN THE SAME MANNER AS VITAMIN B12 AND MAY BE ADMINISTERED IN THE SAME GENERAL DOSAGE RANGES AND BY THE SAME GENERAL ROUTES OF ADMINISTRATION.
Abstract:
A NEW PLASMINOGEN ACTIVATOR DISTINGUISHABLE FROM UROKINASE CAN BE ISOLATED FROM STROMATA OF HUMAN ERYTHROCYTES AT A PH OF FROM ABOUT 1 TO 4. THE PLASMINOGEN ACTIVATOR IS USEFUL FOR THE THERAPY AND PROPHYLAXIS OF THROMBOSES AND EMBOLISMS. THE PLASMINOGEN ACTIVATOR IS ADMINISTERED IN THE FORM OF AN INJECTABLE SOLUTION WHICH CAN BE PREPARED BY TECHNIQUES WHICH ARE PER SE KNOWN IN A THERAPEUTIC DOSAGEOF TE SAME ORDER OF MAGNITUDE AS UROINASE. IT HAS A MOLECULAR WEIGHT AFTER PROCESSING IN THE ULTRACENTRIFUGE BETWEEN ABOUT 20,000 AND 50,000. IT IS A PROTEIN, ACID STABLE TO PH 1 BUT IS ALMOST ENTIRELY DESTROYED AT PH 9-10 AT +4*C. FOR 5 HOURS. IT IS ACTIVATED OR CATALYZED BY SMALL AMOUNTS OF UROKINASE WHICH RAISED ITS ACTIVITY 20-100 FOLD.