Parvalbumin in rat kidney. Purification and localization.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Schneeberger PR,Heizmann CW

doi

10.1016/0014-5793(86)80569-5

subject

Has Abstract

pub_date

1986-05-26 00:00:00

pages

51-6

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(86)80569-5

journal_volume

201

pub_type

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