Abstract: A procedure employed in the purification of anthranilate synhetase of Escherichia coli SJHI is described. The purified anthranilate synthetase appeared to be homogeneous when examined with poliacrylamide gel electrophoresis. Phenly-sepharose CL-4B and Blue dye sepharose were used for purification. A positive correlation was found between purification and ammonium sulfate especially us...

A 130,000 Mr protein was isolated from human platelets by sequential DEAE-Sephacel and Sepharose Cl-4B chromatography. Low shear viscometric measurements showed that the enriched protein after DEAE-Sephacel chromatography inhibited actin polymerization. This effect was somewhat greater in the presence of EGTA than in the presence of calcium. Further purification by Sepharose Cl-4B chromatograph...

Immunosuppressive molecules in uterine fluid from the nonpregnant uterine horn of unilaterally pregnant ewes at Days 60, 100, and 140 of gestation were examined. Uterine fluid from all days inhibited [3H]thymidine incorporation into phytohemagglutinin-stimulated lymphocytes. Inhibitory activity increased with advancing gestation. Uterine fluid also inhibited lymphocyte proliferation caused by o...

The paper reports an efficient procedure for the extraction and purification of R-phycoerythrin (R-PE) from marine red algae Amphiroa anceps. A. anceps was extracted in 50 mM phosphate buffered saline and precipitated by (NH4)2SO4. The R-PE was isolated by ion-exchange chromatography loaded with Q-Sepharose Fast Flow, which was developed by linear ionic strength gradients. Then it was purified ...

We describe here a simple, rapid chromatographic procedure for quantitatively separating serum creatine kinase isoenzymes (EC 2.7.3.2), with diethylaminoethyl (DEAE)-Sepharose CL-6B as the anion-exchanger. We established the column bed height and the elution parameters by use of a simplex procedure. DEAE-Sepharose CL-6B equilibrated in tris(hydroxymethyl)aminomethane (50 mmol/L, pH 7.5, and con...

A previously undescribed bovine serum lectin (designated CL-43) was identified by its Ca(2+)-dependent binding to mannan and by its molecular mass of 43 kDa under reducing conditions on SDS-PAGE. The lectin was isolated by polyethylene glycol precipitation, affinity chromatography on mannan-Sepharose (followed by elution with EDTA), and absorption on Sepharose-4B-coupled rabbit anti-bovine Ig (...

Two protein phosphatases (enzymes I and II) were extensively purified from wheat embryo by a procedure involving chromatography on DEAE-cellulose, phenyl-Sepharose CL-4B, DEAE-Sephacel and Ultrogel AcA 44. Preparations of enzyme I (Mr 197,000) are heterogeneous. Preparations of enzyme II (Mr 35,000) contain only one major polypeptide (Mr 17,500), which exactly co-purifies with protein phosphata...

Proteoglycans extracted from separated specimens of healthy human gingival epithelium and from connective tissue have been purified. The epithelial proteoglycans fractionated as a single included peak on Sepharose 4B-CL and contained heparan sulphate and dermatan sulphate glycosaminoglycans. The connective-tissue proteoglycans separated into three major populations on Sepharose 4B-CL, one of wh...