-transparent.png){kind=logo}
The complete amino acid sequence of calmodulin from wheat germ was determined by isolating and sequencing the cyanogen bromide and tryptic peptides. The protein consisted of 149 amino acid residues and its amino(N)-terminus was blocked with an acetyl group. Wheat germ calmodulin lacked tryptophan and contained 1 mol each of histidine, tyrosine, cysteine, and N epsilon-trimethyllysine residues per mol of the protein. A comparison of its amino acid sequence with that of bovine brain calmodulin indicated that there were eleven amino acid subsitutions other than amide assignments, two insertions and one deletion of amino acid residues in wheat germ calmodulin.
Related Publications
H Toda, and
M Yazawa, and
F Sakiyama, and
K Yagi
June 1967,
The Journal of biological chemistry,
H Toda, and
M Yazawa, and
F Sakiyama, and
K Yagi
May 1982,
Biochemistry,
H Toda, and
M Yazawa, and
F Sakiyama, and
K Yagi
May 1979,
The Biochemical journal,
H Toda, and
M Yazawa, and
F Sakiyama, and
K Yagi
January 1984,
Methods in enzymology,
H Toda, and
M Yazawa, and
F Sakiyama, and
K Yagi
July 1985,
Plant physiology,
H Toda, and
M Yazawa, and
F Sakiyama, and
K Yagi
February 1984,
FEBS letters,
H Toda, and
M Yazawa, and
F Sakiyama, and
K Yagi
December 1983,
Journal of biochemistry,
H Toda, and
M Yazawa, and
F Sakiyama, and
K Yagi
October 1976,
Canadian journal of biochemistry,
H Toda, and
M Yazawa, and
F Sakiyama, and
K Yagi
May 1989,
Biochemistry,
H Toda, and
M Yazawa, and
F Sakiyama, and
K Yagi
January 1963,
Biochimica et biophysica acta,
