Parvalbumin in rat kidney

FEBS Letters

Heizmann, Claus W.¹  Schneeberger, Peter R.¹ 

[1] Institut für Pharmakologie und Biochemie, Universität Zürich-Irchel Winterthurerstrasse 190, CH-8057 Zürich, Switzerland

关键词: Ca2+ binding protein;    Parvalbumin;    Vitamin D;    Calbindin-28 K;    (Kidney);    RIA;    radioimmunoassay;    calbindin-10K/−28K;    vitamin D-dependent Ca2+-binding proteins;    HPLC;    high-performance liquid chromatography;    1D/2D-PAGE;    one-dimensional/two-dimensional polyacrylamide gel electrophoresis;    1α;    25(OH)2D3;    1α;    25-dihydroxycholecalciferol;    PAP;    peroxidase antiperoxidase;   

DOI  :  10.1016/0014-5793(86)80569-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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-28_K. 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.

【 授权许可】

Unknown