Molecular properties and mode of action of homogeneous preparation of stimulatory modulator of cyclic GMP-dependent protein kinase from the heart.
Journal of Biological ChemistryPublished 1 May 1978Open access
Mikio Shoji, Nancy L. Brackett, James Tse, Raymond Shapira, J.F. Kuo
Citations46
SJR quartileQ1
SJR score1.71
SNIP1.00
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TL;DR
The “reassociated’ modulator, obtained by dialysis of the SDStreated factor, was nearly as active as and exhibited the same characteristics of the “native” modulator mentioned.
Abstract
Stimulatory modulator of cyclic GMP-dependent protein kinase was purified to homogeneity from heart extracts. The preparation appeared as a single protein band in the sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis, with a minimal M,. of 34,000, which agreed with the value calculated from its amino acid composition. The modulator was an acidic protein, as indicated by an isoelectric point of about pH 4.0 and a high content of acidic amino acids. It had a Stokes radius of 62 A and a frictional ratio (f/ f,,) of 2.27, indicating that the factor is a highly elongated or asymmetric protein. The modulator exhibited multiple bands in analytical polyacrylamide gel electrophoresis, with each band found to be active. It had a sedimentation coefficient of 2.7 S and a calculated M, of 69,000. The “reassociated” modulator, obtained by dialysis of the SDStreated factor, was nearly as active as and exhibited the same characteristics of the “native” modulator mentioned
Keywords
MedicineBiochemistry, Genetics and Molecular Biology
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