Action of ascorbic acid on a myosin molecule derived from carp.
The influence of L-ascorbic acid at 40 degrees C incubation on the subfragment-1 and rod regions, prepared by chymotryptic digestion of myosin, and myosin was investigated by SDS-polyacrylamide gel electrophoresis and transmission electron microscopy respectively. It was observed that L-ascorbic acid acted more readily on the subfragment-1 region of myosin. Further, circular dichroism measurement indicated that L-ascorbic acid did not affect the structure of myosin. These results suggest that L-ascorbic acid acts more readily on the myosin subfragment-1 region and promotes the gelation of myosin without producing a conformational change in this protein.
Ikeuci
Sayaka
S
Department of Food Science and Nutrition, Doshisha Women's College of Liberal Arts, Kyoto, Japan.
Miyamoto
Yuka
Y
Katoh
Tsuyoshi
T
Nishimura
Kimio
K
D000818:Animals; D001205:Ascorbic Acid / Q000494:pharmacology*; D001665:Binding Sites; D002347:Carps; D004591:Electrophoresis, Polyacrylamide Gel; D008854:Microscopy, Electron; D015879:Myosin Subfragments; D009218:Myosins / Q000737:chemistry* / Q000187:drug effects / Q000378:metabolism; D010449:Peptide Mapping; D011487:Protein Conformation
D015879:Myosin Subfragments; D009218:Myosins; D001205:Ascorbic Acid