TY - JOUR
T1 - Purification and characterization of calmodulin from rat liver mitochondria
AU - Hatase, Osamu
AU - Tokuda, Masaaki
AU - Itano, Toshifumi
AU - Matsui, Hideki
AU - Doi, Akitaka
PY - 1982/1/29
Y1 - 1982/1/29
N2 - Mitochondrial calmodulin of rat liver was purified and classified. It co-migrated with bovine brain calmodulin in non-denaturing polyacrylamide gel electrophoresis, SDS-polyacrylamide gel electrophoresis and isoelectric focusing. The mitochondrial calmodulin activated Ca2+-dependent phosphodiesterase of bovine brain in the presence of Ca2+. About 80% of the mitochondrial calmodulin was proved to be of cytosol origin. It was easily detached by washing with buffer containing EGTA. The other 20% was intramitochondrial calmodulin; half of it was in the matrix space, and half in the membrane.
AB - Mitochondrial calmodulin of rat liver was purified and classified. It co-migrated with bovine brain calmodulin in non-denaturing polyacrylamide gel electrophoresis, SDS-polyacrylamide gel electrophoresis and isoelectric focusing. The mitochondrial calmodulin activated Ca2+-dependent phosphodiesterase of bovine brain in the presence of Ca2+. About 80% of the mitochondrial calmodulin was proved to be of cytosol origin. It was easily detached by washing with buffer containing EGTA. The other 20% was intramitochondrial calmodulin; half of it was in the matrix space, and half in the membrane.
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U2 - 10.1016/0006-291X(82)90689-1
DO - 10.1016/0006-291X(82)90689-1
M3 - Article
C2 - 6280700
AN - SCOPUS:0020493095
SN - 0006-291X
VL - 104
SP - 673
EP - 679
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -