Purification of Hyaluronidase. II

Purification and partial characterization of testicular hyaluronidase.

A new method is presented for the purification of testicular hyaluronidase involving ion exchange chromatography followed by gel filtration on Sephadex G-75. A highly purified hyaluronidase preparation has been obtained which contains 45,000 National Formulary activity units per mg, dry weight, and which migrates as a single component on polyacrylamide gel electrophoresis at pH 4.3. The enzyme ...

The Purification of Hypertensin Ii

The enzymatic conversion of hypertensin I to hypertensin II is described together with the subsequent purification of the product by means of counter-current distribution. Improved methods are also presented for the preparation of renin and its substrate, as well as in methods for the reaction of these materials and the purification of the resulting hypertensin I.

Heparin-sepharose affinity chromatography for purification of bull seminal-plasma hyaluronidase.

Bull seminal-plasma hyaluronidase was purified 180-fold by chromatography on concanvalin A-Sepharose, heparin Sepharose, Sephadex G-200 and Sephacryl S-200. With hyaluronic acid as the substrate, the specific activity and turnover number of purified hyaluronidase were 3.63 mumol/min per mg (104000 National Formulary units/mg of protein) and 214 min-1 (mol of product formed/mol of enzyme per min...

Optimized Method for Purification of Expressed Plasmodium Vivax Duffy Binding Protein-II (PvDBP-II): Implication for Vivax Malaria Vaccine Development

  Background: The purity and correct folding of a recombinant protein is critical for any structural, biochemical and vaccine design studies. Plasmodium vivax Duffy binding protein-II is a leading vaccine candidate for vivax malaria. In the present study, the purification process of recombinant DBP-IX (a variant form of PvDBP-II) was optimized to achieve the highest yield and purity. Moreover, ...

Crystal structure determination of hyaluronidase, a major bee venom allergen, in complex with an IgG Fab fragment and purification and biophysical characterization of bovine testes hyaluronidase