Perch muscle parvalbumin: general characterization and magnesium-binding properties.

1. Parvalbumin exists in two major forms, amounting to 2.5 and 3.

Comparative properties of vertebrate parvalbumins.

Pure parvalbumins isolated from turtle, chicken, and rabbit white skeletal muscle have been characterized in terms of their physical, chemical, and immunological properties. As for the parvalbumins of most fish and amphibians, they have sedimentation constants S20,w of approximately 1.45 +/- 0.

On the subunit structure of particulate aminopeptidase from pig kidney.

Solubilization of particulate aminopeptidase (EC 3.4.11.