An endoglycosidase which cleaves heparin and heparan sulfate was isolated from outdated human platelets by freeze-thaw solubilization, heparin-Sepharose chromatography, DEAE-cellulose chromatography, hydroxylapatite chromatography, octyl-agarose chromatography, concanavalin A-Sepharose chromatography, and Sephacryl S-200 gel filtration. The overall extent of purification of the platelet heparit...

To facilitate the diagnosis of recent rubella infection, rubella haemagglutination inhibiting antibody has been determined in four fractions obtained by Sephadex G-200 gel filtration of samples of serum. All the 21 samples collected at the convalescent stage of the disease had varying proportions of haemagglutination inhibiting antibody in fraction 1, representing the major portion of IgM antib...

A 15 kDa ribonuclease (RNase) was purified from dried fruiting bodies of the wild edible mushroom Armillaria luteo-virens. The simple 4-step purification protocol involved ion-exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion-exchange chromatography on SP-Sepharose and a final gel filtration by FPLC on Superdex-75. The RNase was unadsorbed on Affi-gel ...

A deoxyribonuclease distinct from the previously isolated asparagus ribosome-inactivating proteins, possessing a molecular weight of 30 kDa and requiring a pH of 7.5 for optimum hydrolytic activity toward herring sperm DNA, was isolated from Asparagus officinalis seeds. The isolation procedure involved extraction with saline, (NH(4))(2)SO(4) precipitation, ion-exchange chromatography on DEAE-ce...

conclusions the elevation of hmw-alp activity in cu treated animal suggests the occurrence of biliary disease. this may be used as a biomarker for the diagnosis of copper toxicity. results obtained data showed that with increasing administration of copper, the alp activity was elevated significantly. in comparison with the control group the elevations were between 20%-56% using gel filtration c...

Riboflavin-binding protein (RfBP) was isolated, purified and characterized from Coot (Fulica atra) egg. The RfBP was purified using DEAE-Sepharose ion exchange chromatography followed by gel filtration on Sephadex G-100. The purity of the proteins was judged by SDSPAGE. The protein migrated as a single band on SDS gel with a molecular weight of corresponding to nearly 29 Kd.

Beta-toxin was purified about 340-fold from culture supernatant fluid of Clostridium perfringens type C with a yield of about 24% in terms of biologically active beta-toxin. The purification involved ammonium sulfate fractionation, gel filtration through Sephadex G-100, isoelectrofocusing in a pH 3 to 6 gradient, and immunoaffinity chromatography. The purified beta-toxin gave a single band on p...