Aminoethyl Cellulose Research Articles

Preparation of enzymically active, water-insoluble derivatives of trypsin

Insoluble trypsin has been prepared by the use of glutaraldehyde to effect intermolecular crosslinks. Glutaraldehyde was also used to conjugate trypsin to aminoethyl cellulose with production of an insoluble preparation. Insoluble trypsins thus prepared exhibited enzymic activity toward casein.

L'application des radioisotopes à la chromatographie sur colonnes de celluloses substituées—I

Cellulose powder, carboxymethyl cellulose, aminoethyl cellulose, diethylaminoethyl cellulose and cellulose phosphate have found application for column chromatography with organic solvents. The quantitative adsorption and elution of microgram amounts of cobalt have been accomplished. Cobalt-60 tracer has been used and estimated by gamma-ray spectrometry. It has been shown that the strength of adsorption of cobalt depends on the special functional groups attached to the modified celluloses.

Purification of Activated Bovine Hageman Factor

SummaryActivated Hageman Factor has been purified 3000 to 5000 fold from citrated bovine plasma as measured in a thoroughly devised assay procedure. The steps of purification include adsorption on aluminium hydroxide gel, glass, diethyl- aminoethyl cellulose and Sephadex G-200. A fractionation according to Cohn between step 2 and 3 renders the factor more stable for further purification. The purified preparations corrected the clotting defect in human plasma with Hageman trait. The most purified fractions were devoid of plasma thromboplastin antecedent (PTA), other clotting factors.

A Rapid Method of preparing Pure Serum Gamma-Globulin

IN the course of investigating various methods of isolating skin-sensitizing antibodies from human allergic serum, a procedure has been devised which could be applied to the rapid preparation of other 7S-type gamma-globulins in a high degree of purity. The technique employs diethyl amino ethyl cellulose anion exchanger, prepared according to the method used by Peterson and Sober1, to adsorb out of the serum all proteins other than 7S-type gamma-globulins. For this purpose, a batch process has proved superior to the more widely used column chromatography, because of its greater speed and ease of manipulation.

Chromatography of Rat Liver Soluble Proteins and Localization of Enzyme Activities

SUMMARY A method was developed for chromatography of rat liver soluble proteins on diethylaminoethyl cellulose, with a parabolic chloride gradient for elution. Protein, nucleic acid and 16 en- zyme activities were determined in the fractions, and each gave a consistent pattern of distribution in a number of preparations. Some of the enzyme activities, for example, lactic dehydro- genase, isomerase, and aldolase, were not adsorbed by the diethyl- aminoethyl cellulose at pH 8.0 and low ionic strength. Several of the enzymes gave multiple peaks of activity. With two of multiple peak enzymes, glucose 6-phosphate dehydrogenase and glutamic oxaloacetic transaminase, rechromatography of one of the peaks, under the same conditions, gave a single peak at the anticipated position. REFERENCES 1. SOBER, H. A., GUTTER, F. J., WYCOFF, M. M., AND PETERSON, E. A., .Z. Am. Chem. Sac., ‘78, 756 (1956). 2. SOBER,

Studies on the Small Particle Complement-Fixing Antigen of Foot-and-Mouth Disease Virus

SummaryThe so-called small particle CF-antigen fraction, free of infectious virus particles and larger components, was prepared by centrifugation from bovine tongue epithelium infected with FMDV, type A, strain 119. The CF activity of this fraction was stable through the pH range of 5.25 to 10.5, withstood heating for 30 minutes at 60°C, and was resistant to the action of proteolytic and nucleolytic enzymes. It was precipitated by dialysis and by ammonium sulfate, ethanol, and acetone. Diethyl amino ethyl cellulose and calcium phosphate columns prepared at different ionic strengths were used in chromatographic purification. The small particle CF-antigen displays the properties of a euglobulin and is appreciably more stable than the large infective particle with which it is associated.