TY - JOUR
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.
UR - http://www.scopus.com/inward/record.url?scp=0026608008&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026608008&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(92)91888-W
DO - 10.1016/0006-291X(92)91888-W
M3 - Article
C2 - 1540183
AN - SCOPUS:0026608008
VL - 182
SP - 1395
EP - 1401
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -