Angiotensin I-converting enzyme inhibitory peptides derived from bonito bowels autolysate.
Six angiotensin I-converting enzyme inhibitory peptides were isolated from a bonito bowels autolysate. Their amino acids were sequenced as Tyr-Arg-Pro-Tyr, Gly-His-Phe, Val-Arg-Pro, Ile-Lys-Pro, Leu-Arg-Pro, and Ile-Arg-Pro. Peptides having corresponding amino acid sequences were synthesized by a solid-phase method and their inhibition of the activity measured. IC50 of these peptides were estimated to be 320, 1100, 2.2, 2.5, 1.0, and 1.8 microM, respectively. The role of carboxyl terminal proline residues on the inhibition is discussed.
Matsumura
N
N
Foods Division, Asahi Chemical Industry Co., Ltd. Shizuoka, Japan.
Fujii
M
M
Takeda
Y
Y
Sugita
K
K
Shimizu
T
T
D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000138:chemical synthesis / Q000737:chemistry / Q000302:isolation & purification*; D000818:Animals; D005399:Fishes; D007422:Intestines / Q000737:chemistry*; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry / Q000302:isolation & purification*
D000806:Angiotensin-Converting Enzyme Inhibitors; D009842:Oligopeptides