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Fig. 3. (A) Western blot on muscle homogenates enriched in myofibrillar proteins
from infected (i) and healthy (h) individuals, probed with a monoclonal
antibody to Drosophila MHC. Lanes contain identical protein
concentrations. Aside from the 206 kDa muscle MHC and non-specific reactivity
to some high-molecular-mass proteins, a 165 and 155 kDa protein were
identified. Left tick marks represent molecular mass standards (lane not
shown). The presence of 165 and 155 kDa bands in infected muscle indicates
that this may be a relatively `high-powered' infected individual, as shown in
Fig. 5E. However, no
performance measures were obtained from this individual's muscles. (B)
Silver-stained SDS-PAGE gel showing peptides obtained by calpain (lane b)
digestion of purified L. pulchella MHC from both healthy and infected
individuals (lane a). In calpain-treated samples, a 156 kDa peptide can be
observed, as well as a 122 and 110 kDa peptide. In addition, we putatively
identified a calpain 80 kDa subunit, and other bands as calpain
autodegradation products [i.e. similar to results reported by Pemrick and
Grebenau (Pemrick and Grebenau,
1984)].
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