Acidic calmodulin binding protein, ACAMP-81, is MARCKS protein interacting with synapsin I

Akihiro Mizutani, Hiroshi Tokumitsu, Hiroyoshi Hidaka

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

ACAMP-81 is an acidic calmodulin binding protein with molecular mass of 81 kDa. We report partial amino acid analysis of ACAMP-81 and its interaction with synapsin I. 123 amino acids of ACAMP-81 were determined and the sequence was completely identical with that of MARCKS protein which was thought to be a substrate for calcium/phopholipid dependent protein kinase (PKC). We found ACAMP-81 bound to synapsin I with 125I-labeled ACAMP-81 overlay method. ACAMP-81 bound to the cysteine specific cleaved 51 kDa fragment derived from middle/tail region of synapsin I.

Original languageEnglish
Pages (from-to)1395-1401
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume182
Issue number3
DOIs
Publication statusPublished - Feb 14 1992
Externally publishedYes

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Synapsins
Calmodulin-Binding Proteins
Amino Acids
Molecular mass
myristoylated alanine-rich C kinase substrate
Cysteine
Substrates

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Acidic calmodulin binding protein, ACAMP-81, is MARCKS protein interacting with synapsin I. / Mizutani, Akihiro; Tokumitsu, Hiroshi; Hidaka, Hiroyoshi.

In: Biochemical and Biophysical Research Communications, Vol. 182, No. 3, 14.02.1992, p. 1395-1401.

Research output: Contribution to journalArticle

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