Action of ascorbic acid on a myosin molecule derived from carp

The influence of L-ascorbic acid at 40 deg 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 ac...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2007-08, Vol.71 (8), p.2091-2094
Main Authors: Ikeuci, S.(Doshisha Women's Coll. of Liberal Arts, Kyoto (Japan)), Miyamoto, Y, Katoh, T, Nishimura, K
Format: Article
Language:English
Subjects:
ACIDE ASCORBIQUE
ACIDO ASCORBICO
Animals
ASCORBIC ACID
Ascorbic Acid - pharmacology
Binding Sites
Biological and medical sciences
CARP
CARPA
CARPE
Carps
Cyprinidae
Electrophoresis, Polyacrylamide Gel
Freshwater
Fundamental and applied biological sciences. Psychology
gelation
improvement mechanism
Microscopy, Electron
MIOSINA
MYOSIN
Myosin Subfragments
MYOSINE
Myosins - chemistry
Myosins - drug effects
Myosins - metabolism
Peptide Mapping
Protein Conformation
subfragment-1
vitamin C
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Summary:The influence of L-ascorbic acid at 40 deg 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.
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.70205