High abundance calmodulin from Blattella germanica eggs binds to vitellin subunits but disappears during vitellin utilization
1992
Zhang, Y. | Kunkel, J.G.
A Ca2+-binding protein has been purified and characterized from Blattella germanica eggs. This protein has biochemical features in common with calmodulin (CaM). These common features include a relative low molecular weight of approximately 19 kDa, thermal stability, an acidic pI of 4.0, a low specific absorbance (E277nm 1% = 2.9), an altered electrophoretic mobility in SDS-polyacrylamide gels in the presence of 1 mM Ca2+, and calcium-dependent binding to the CaM antagonist W-7. These features, considered together with activation of CaM-dependent phosphodiesterase in a Ca2+-dependent manner and cross-reactivity with anti-bovine brain CaM antibody, are sufficient to define this protein as bone fide CaM. CaM comprises 1-1.5% of soluble protein of newly ovulated eggs depending on the mode of assay. A rabbit antibody specific for the B. germanica CaM cross-reacts with bovine brain CaM. 14C-labeled cockroach CaM in a gel-overlay technique binds to vitellin, the major yolk protein of B. germanica egg. The CaM-binding site of vitellin is located on the 95 kDa subunit before degradation and 53 kDa fragment after 95 kDa subunit breakdown. There is sufficient CaM to bind stoichiometrically (1:1) with the vitellin trimer. CaM is present at uniformly high levels until vitellin utilization starts then it is undetectable until the pharate larval stage at the end of embryogenesis.
اظهر المزيد [+] اقل [-]الكلمات المفتاحية الخاصة بالمكنز الزراعي (أجروفوك)
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