Conformationally altered aortic myosin light chains

Meei Jyh Jiang, Lan King, Yuh Jen Chao

Research output: Contribution to journalArticle

Abstract

Aorta smooth myosin contains two types of light chain, LC20 and LC17, which fold together with the N-terminal region of each heavy chain to form the globular head region of myosin. We demonstrate an altered conformation of LC20 after its separation from heavy chain by high concentrations of urea, on the basis of the following evidende: 1) A polyclonal antibody against LC20 was not able to recognize this conformationally altered form; 2) Myosin reconstituted from heavy chains and urea-dissociated light chains exhibited extremely low ATPase activity. Circular dichroism unfolding profiles showed that light chains dissociated from heavy chains by SDS appeared to be more stable than those generated by urea dissociation.

Original languageEnglish
Pages (from-to)113-116
Number of pages4
JournalMolecular and Cellular Biochemistry
Volume136
Issue number2
DOIs
Publication statusPublished - 1994 Jul 1

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Clinical Biochemistry
  • Cell Biology

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