The cellulose ion exchangers (1) have proved to be useful chromatographic media for the serum proteins. In the fractionation of normal human serum on the anion exchanger, diethylaminoethyl (DEAE) cellulose, application of buffer gradients of increasing concentration and decreasing pH results in the appearance of components in the effluent fluid in order of increasing electrophoretic mobility (2...

The partial purification of beef thyrotropin with the cation exchangers Amberlite IRC-50 (2, 3) and carboxymethyl (CM) cellulose (3, 4) has been previously reported. The preceding paper (5) describes the rechromatography on diethylaminoethyl (DEAE) cellulose of thyrotropin preparations assaying 20 U.S.P. units per mg which resulted in fractions apparently containing only those glycoproteins wit...

A procedure was devised for isolating human pepsins 1, 2, 3 and 5 from gastric juice by repetitive column chromatography on DEAE-cellulose. The combined yields in four different experiments varied from 14% to 90% of the total peptic activity of the starting material. The isolated individual pepsins were shown to behave as single homogeneous proteins on agar-gel electrophoresis at pH 5.0 and on ...

Normal human serum has been shown' to exhibit cholesterol-binding properties upon immunoelectrophoresis on agar gel. The evidence clearly supports the concept of a specific type of binding of cholesterol by alpha-beta globulin. Accordingly, the name "transcholesterin" was proposed for the reactive component. In order to evaluate the mechanism of in vitro interaction of cholesterol with transcho...

The relative amounts of two valyl-tRNA species from Bacillus subtilis W23 were compared by methylated albumin Kieselguhr column chromatography and by diethylaminoethyl cellulose column chromatography after T1 ribonuclease digestion. The ratio of the two valyl-tRNAs changes significantly during sporulation, during step-up and step-down growth transitions, during the stationary phase of an asporo...

Pollen is an excellent source of actin for biochemical and physiological studies of the actomyosin system in higher plants. We have developed an efficient method to prepare relatively high levels of actin from the pollen of maize (Zea mays L.). The procedures of purification include acetone powder preparation, saturated ammonium sulfate fractionation, diethylaminoethyl-cellulose chromatography,...

An enzyme which catalyzes the hydrolytic cleavage of various ribonucleosides to free base and ribose components has been obtained from cells of Pseudomonas fluorescens and purified about 300-fold by fractionation with protamine sulfate, ammonium sulfate, alumina Cy, and diethylaminoethyl cellulose. The preparation thus purEed catalyzes the hydrolysis of about 50 moles of uridine per min per mg ...

We have modified the columti-chromatographic technique of Mercer (1) to produce a sensitive and rapid separation of serum CK2 and CK3, even at normal total serum CK activity (3).12 However, CKj was not separated from CK2. Here, we report a modification of our method such that all three CK isoenzymes are separated by stepwise elution from a mini-column of diethylaminoethyl-cellulose. CK1 has onl...