Parvalbumin in rat kidney. Purification and localization.
The Ca2+-binding parvalbumin has been purified for the first time from rat kidney. Its biochemical and immunological properties were indistinguishable from the muscle counterpart. By immunohistochemical methods parvalbumin was localized in part of the distal tubule and proximal collecting duct, similar to the vitamin D-dependent Ca2+-binding protein, calbindin-28K. Parvalbumin was found to be independent of the vitamin D status of the animal since its concentration remained unchanged in kidney extracts of normal, rachitic and vitamin D-replete rats. Both proteins may be involved in the regulation of intracellular Ca2+ in kidney.
D000818:Animals; D002845:Chromatography; D003101:Collodion; D004591:Electrophoresis, Polyacrylamide Gel; D006651:Histocytochemistry; D007124:Immunoenzyme Techniques; D007158:Immunologic Techniques; D007668:Kidney / Q000032:analysis*; D007685:Kidney Tubules, Collecting / Q000032:analysis; D007686:Kidney Tubules, Distal / Q000032:analysis; D009124:Muscle Proteins / Q000032:analysis*; D009132:Muscles / Q000032:analysis; D010320:Parvalbumins / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis; D051381:Rats; D012279:Rickets / Q000188:drug therapy / Q000378:metabolism; D014807:Vitamin D / Q000627:therapeutic use
D009124:Muscle Proteins; D010320:Parvalbumins; D010446:Peptide Fragments; D014807:Vitamin D; D003101:Collodion