Uroporphyrinogen III synthase purified from rat liver is a monomer of Mr 36,000 by gel filtration and 28,000 by SDS/polyacrylamide-gel electrophoresis. The enzyme exists in two interconvertible forms separable on h.p.l.c. Both forms of the enzyme could be renatured with full activity after SDS/polyacrylamide-gel electrophoresis, demonstrating the absence of a reversibly bound cofactor. The enzy...

An anti-epilepsy peptide (AEP) was isolated and purified from venom of the scorpion Buthus martensii Karsch. The purification procedure included CM-Sephadex C-50 chromatography, gel filtration on Sephadex G-50 and DEAE-Sephadex A-50 chromatography. Its homogeneity was demonstrated by pH 4.3 polyacrylamide-disc-gel electrophoresis, focusing electrophoresis and SDS/polyacrylamide-disc-gel electro...

INTRODUCTION SDS-polyacrylamide gel electrophoresis (SDS-PAGE) represents the second-dimension separation of two-dimensional (2D)-PAGE. Large-scale proteome analysis usually requires simultaneous electrophoresis of batches of second-dimension SDS-PAGE gels to maximize the reproducibility of 2D electrophoresis protein profiles. This requirement is most easily met using multiple, vertical second-...

Aim. To search fibrinogenolytic enzymes among protein components of Vipera renardi snake venom. Methods. Venom V. as the lyophilized powder was supplied by Trypillia serpentarium. It dissolved in 0.05 M Tris-HCl buffer pH 8.3 and fractionated on Superdex G-75 using FPLC system Acta Prime. Peaks were tested for their ability to directly cleave fibrinogen. Hydrolytic products analyzed SDS-PAGE. E...

the effects of sodium n-dodecyl sulphate (sds) on the structure of histone hi has been studied by a combination of e:quilibrium dialysis, u.v. spectroscopy ; polyacrylamide gel electrophoresis, protein titration and viscometery techniques using, 2.5 mm phosphate buffer, ph 6.4. the interaction of h, and sds in contrast tomanyothel-protein-sds interactions is organized between v 40 to 70. above ...

The effects of sodium n-dodecyl sulphate (SDS) on the structure of histone HI has been studied by a combination of e:quilibrium dialysis, U.V. spectroscopy ; polyacrylamide gel electrophoresis, protein titration and viscometery techniques using, 2.5 mM phosphate buffer, pH 6.4. The interaction of H, and SDS in contrast tomanyothel-protein-SDS interactions is organized between V 40 to 70. A...