0000000000696992
AUTHOR
Gilbert Turian
Calmodulin-stimulated cyclic nucleotide phosphodiesterase from Neurospora crassa.
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Immunopurification of highly specific antibodies against calmodulin from Neurospora crassa
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Calcium, calmodulin-dependent protein phosphorylation in Neurospora crassa
Abstract A calcium, calmodulin-dependent protein kinase activity has been partially purified by calmodulin-Sepharose affinity chromatography from the soluble fraction of Neurospora crassa . The phosphorylated peptide has an apparent molecular mass on SDS-polyacrylamide gel of 47 kDa. The apparent half maximal phosphorylation is obtained after 1.5 min at 30° C in the presence of calcium and calmodulin. The apparent half maximal activation of the phosphorylation is obtained at 1 μM calcium, and 0.1 or 0.2 μM calmodulin from bovine brain or Neurospora , respectively. The 32 P incorporation is enhanced about 10-fold by calmodulin.
A search for myosin in elongating hyphae of Neurospora crassa
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Changed protein pattern during heat shock and conidiogenous shift in Neurospora crassa
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Actin in Allomyces arbuscula
International audience; A 42 kDa protein was isolated by affinity chromatography on DNAse I-Sepharose from 24-h-old mycelia of Allomyces arbuscula. It was identified as actin by immunoblots with monoclonal antibody probe against a chicken gizzard actin. This fungal actin has a pI of 5.9 and separates into two spots on two-dimensional polyacrylamide gel electrophoresis, suggesting its dual nature. It can polymerize into 8-10 nm filaments visualized by electron microscopy.