Calbindin D(28K) forms a Ca2+-dissociable complex with mellitin in vitro

Vincenzo La Bella, Bao Kuang Ho, Stanley H. Appel, Robert G. Smith

Research output: Contribution to journalArticle

6 Scopus citations

Abstract

Calbindin D(28K) (CB), a cytosolic calcium binding protein (CBP), forms a macromolecular complex with the polypeptide mellitin (ME) the absence of calcium, which can be reversibly dissociated by the addition of Ca2+. The molar ratio of CB:ME constituted in this complex is 1:4, suggesting that CB interacts with the tetrameric form of ME. Like free tetrameric ME, the CB:ME complex does not migrate into 15% non-denaturing polyacrylamide electrophoretic gels, although both constituents migrate normally after irreversible complex denaturation by heating in sodium dodecyl sulphate (SDS). The interaction of these two proteins can be distinguished from the association of calmodulin (CM) with ME, which forms a reversibly dissociable, equimolar complex in the presence of Ca2+ and a stable non-migrating complex (molar ratio = 1:12) in its absence. Thus, CB and CM appear to bind ME under different Ca2+ regulatory control, suggesting possible roles for CB as a Ca2+-dependent regulatory binding protein.

Original languageEnglish (US)
Pages (from-to)1199-1210
Number of pages12
JournalBiochemistry and Molecular Biology International
Volume38
Issue number6
StatePublished - Jan 1 1996

Keywords

  • Calbindin D(28K)
  • Calcium
  • Calmodulin
  • Mellitin
  • Parvalbumin

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Molecular Biology

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