Unknown

Dataset Information

0

The preparation of calmodulins from barley (Hordeum sp.) and basidiomycete fungi.


ABSTRACT: 1. Calmodulin-like proteins were purified from the fruiting bodies of higher (basidiomycete) fungi and barley (Hordeum sp.) shoots. 2. These calmodulins have electrophoretic mobilities on 10% (w/v) polyacrylamide gels at pH 8.3 in the presence of 6 M-urea and at pH 8.3 in the presence of 0.1% sodium dodecyl sulphate similar to that of bovine brain calmodulin. They interacted with rabbit skeletal-muscle troponin I in the presence of Ca2+. 3. Barley and fungal calmodulins activated myosin light-chain kinase and phosphodiesterase in the presence of Ca2+, although the amounts needed were at least an order of magnitude greater than is required to produce the same effect with mammalian calmodulin. 4. Amino acid analyses indicated a number of differences from the mammalian protein, most notably the absence of trimethyl-lysine. 5. By using 125I-labelled calmodulin, a small amount of calmodulin-binding protein was detected in homogenates of barley and fungi. 6. No protein corresponding to calmodulin could be found in Escherichia coli or yeast, although a relatively high concentration of a protein that bound calmodulin was detected in E. coli by this technique.

SUBMITTER: Grand RJ 

PROVIDER: S-EPMC1161454 | biostudies-other | 1980 Mar

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC6158276 | biostudies-literature
2022-01-16 | GSE185548 | GEO
| S-EPMC7272565 | biostudies-literature
| S-EPMC8570957 | biostudies-literature
| S-EPMC3998117 | biostudies-literature
2011-11-23 | GSE33773 | GEO
| S-EPMC1220540 | biostudies-other
| S-EPMC3153672 | biostudies-literature
| S-EPMC7412030 | biostudies-literature
| S-EPMC3080886 | biostudies-literature