Irradiated proteins may be converted to higher-molecularweight
aggregates due to the generation of inter-protein crosslinking
reactions, hydrophobic and electrostatic interactions and
the formation of disulphide bonds (Le Maire et al., 1990). Our study
shows that irradiation, even up to a dose of 3 kGy, did not noticeably
induce the aforementioned degradation processes. However, a
slight decrease in the myosin heavy chain content (MHC, 200 kDa,
Fig. 4A) was observed as the irradiation dose increased. With respect
to other protein patterns, the number of bands did not
change in either the non-irradiated or irradiated samples. This phenomenon
may indicate that low E-beam irradiation dosages have
little effect on the molecular weight of different protein bands.
Irradiated proteins may be converted to higher-molecularweight
aggregates due to the generation of inter-protein crosslinking
reactions, hydrophobic and electrostatic interactions and
the formation of disulphide bonds (Le Maire et al., 1990). Our study
shows that irradiation, even up to a dose of 3 kGy, did not noticeably
induce the aforementioned degradation processes. However, a
slight decrease in the myosin heavy chain content (MHC, 200 kDa,
Fig. 4A) was observed as the irradiation dose increased. With respect
to other protein patterns, the number of bands did not
change in either the non-irradiated or irradiated samples. This phenomenon
may indicate that low E-beam irradiation dosages have
little effect on the molecular weight of different protein bands.
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