Calmodulin and rat vitamin D-dependent calcium-binding proteins: Biochemical and immunochemical comparison

Sylvia Christakos, M. Elizabeth, H. Bruns, Aruna S. Mehra, William B. Rhoten, Linda J. Van Eldik

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


Purified vitamin D-dependent rat intestinal (Mr 10,000) and rat renal (Mr 28,000) calcium-binding proteins (CaBPs) have been compared to vertebrate calmodulin, and the vitamin D-dependent CaBPs have been found to be distinct from calmodulin by biochemical and immunochemical criteria. Rat renal and rat intestinal CaBPs do not stimulate 3′,5′-cyclic nucleotide phosphodiesterase, do not compete with iodinated calmodulin for binding to phenothiazine-Sepharose conjugates, do not cross-react immunochemically, and do not contain Nε{lunate}-trimethyllysine. In addition, although calmodulin exhibits a characteristic calcium-dependent mobility shift on polyacrylamide gels in the presence of sodium dodecyl sulfate, a similar mobility shift is not observed for the vitamin D-dependent CaBPs. Immunocytochemically, calmodulin has a widespread localization in the kidney, whereas CaBP is present specifically in the distal tubules of the kidney. These localizations suggest a specialized role for CaBP in the kidney. Thus, although the vitamin D-dependent CaBPs and calmodulin are similar in that they are small, acidic, calcium-binding proteins, these two classes of proteins are biochemically and immunochemically distinct.

Original languageEnglish (US)
Pages (from-to)38-47
Number of pages10
JournalArchives of Biochemistry and Biophysics
Issue number1
StatePublished - May 15 1984

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology


Dive into the research topics of 'Calmodulin and rat vitamin D-dependent calcium-binding proteins: Biochemical and immunochemical comparison'. Together they form a unique fingerprint.

Cite this