Purification of soluble guanylyl cyclase from bovine lung by a new immunoaffinity chromatographic method.

@article{Humbert1990PurificationOS,
  title={Purification of soluble guanylyl cyclase from bovine lung by a new immunoaffinity chromatographic method.},
  author={Pascale Humbert and Feraydoon Niroomand and Gunter Fischer and B Mayer and Doris Koesling and K D Hinsch and Heinrich Gausepohl and Ronald M Frank and Guenter Schultz and Eycke B{\"o}hme},
  journal={European journal of biochemistry},
  year={1990},
  volume={190 2},
  pages={273-8}
}
Soluble guanylyl cyclase was purified from bovine lung by an immunoaffinity chromatographic method using IgG fractions of antisera against a synthetic peptide of the C-terminus of the 70-kDa subunit of the enzyme. After anion-exchange chromatography, the enzyme was bound to an immunoaffinity column and was eluted with the synthetic peptide. This method allowed the convenient isolation of 2 mg of apparently homogeneous enzyme from 40 g cytosolic proteins. The enzyme had an apparent molecular… CONTINUE READING