1. Isoelectric focusing of human liver alkaline phosphatase in a sucrose density gradient with LKB Ampholine as carrier ampholytes is described. 2. Problems due to the chelating properties of the ampholytes and the pH gradient were examined. 3. A reactivation procedure to counter these effects was devised that can probably be used for other alkaline phosphatases. 4. The isoelectric point of hum...

1. Rabbits were immunized with Bact. typhosum 0 901 S and 0 901 R, over a long period. Homologous and heterologous strains were sensitized with sera obtained from weekly bleedings. Agglutination titer was recorded, and the isoelectric points of the bacteria maximally sensitized were determined. 2. 0 901 S maximally sensitized with homologous immune serum had isoelectric points which became more...

1. The behaviour of choline acetyltransferase from pigeon, guinea-pig, rat and cat brain on isoelectric focusing was studied. 2. Choline acetyltransferase from pigeon and guinea-pig brain showed single peaks with isoelectric points at pH6.6 and 6.8 respectively. Only one molecular form of the enzyme was therefore detected in these species. 3. Three peaks of choline acetyltransferase activities ...

I. A third isoenzyme of soybean lipoxygenase (linoleate: oxygen oxidoreductase, EC 1.13.I.13) has been purified to essential homogeneity by Sephadex DEAEA5o column chromatography and isoelectric focusing. 2. The enzyme differs from the two previously described pure isoenzymes (lipoxygenases-i and -2) 1 by the following criteria: elution profile from DEAESephadex, isoelectric point, pH activity ...

A protein with potent cell-attachment and spreading-promoting activity was isolated from fibronectin-free human serum. The purification steps included affinity chromatography on heparin-agarose and preparative isoelectric focusing. The purified protein was homogeneous as judged from dodecyl sulphate/polyacrylamide-gel electrophoresis. It had an isoelectric point of 5.0 and an Mr of 52 000. The ...

A cohaemolysin from the culture supernate of a canine pathogenic group G streptococcus (S. canis) was purified to electrophoretic homogeneity. The purification procedure involved ammonium sulphate precipitation, ultrafiltration, gel filtration and preparative isoelectric focusing. The cohaemolysin consisted of a single polypeptide chain, 18.6 kDa, with an isoelectric point at pH 5.1. The protei...