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

Akihiro Mizutani; Hiroshi Tokumitsu; Hiroyoshi Hidaka

doi:10.1016/0006-291X(92)91888-W

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

Akihiro Mizutani, Hiroshi Tokumitsu, Hiroyoshi Hidaka

Research output: Contribution to journal › Article › peer-review

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 language	English
Pages (from-to)	1395-1401
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	182
Issue number	3
DOIs	https://doi.org/10.1016/0006-291X(92)91888-W
Publication status	Published - Feb 14 1992
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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

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.",

author = "Akihiro Mizutani and Hiroshi Tokumitsu and Hiroyoshi Hidaka",

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doi = "10.1016/0006-291X(92)91888-W",

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T1 - Acidic calmodulin binding protein, ACAMP-81, is MARCKS protein interacting with synapsin I

AU - Mizutani, Akihiro

AU - Tokumitsu, Hiroshi

AU - Hidaka, Hiroyoshi

PY - 1992/2/14

Y1 - 1992/2/14

N2 - 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.

AB - 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.

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DO - 10.1016/0006-291X(92)91888-W

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AN - SCOPUS:0026608008

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EP - 1401

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

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

Abstract

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