By Anthony R. Means, P. Michael Conn (Eds.)
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26) had molecular weights of 30,000 and 33,000 on SDS gels, indicating that they may occur as tetramers in the native state. It is not clear if they are made of identical or nonidentical subunits. But a closer examination of this region shows an initial high concentration of 33K and gradual appearance of 30K proteins. This may suggest that there are two heavy molecular weight forms, each composed of identical subunits. 2) (Fig. 1). Practically all the 33K calcimedin was distributed almost equally between 50 and 150 mM NaC1 eluents while >90% of 30 K calcimedin appeared in 50 mM NaC1 eluent.
Bacterial lysates). Since CaM contains no free sulfhydryl groups, the use of the organomercurial columns selectively removes "nonspecific" protein contaminants which bind melittin-Sepharose as well as thiol-containing proteins exhibiting higher affinity interactions such as S-100 protein. , increasing the ratio of tissue to affinity gel); indeed, a single-step purification from testis supernatant, without organomercurial agarose, was achieved by just saturating the binding capacity of a gel which had been used repeatedly (Fig.
8. All hydrophobic affinity chromatography steps are carried out at 4°. Depending on the tissue source the eluent contains a mix of proteins, the most prominent of which have molecular weights of 32,500 and 67,000. 1% SDS and distilled water, followed by the loading buffer. The individual calelectrins can be purified from the EGTA-eluent by several methods. Gel Filtration. Any column with a separation range of 10 to 100 kDa will be suitable, but we found an AcA 44 column especially effective. 4, the calelectrins behave like monomers on these columns with Stokes radii corresponding to their monomeric molecular weights.
Cellular Regulators Part A: Calcium- and Calmodulin-Binding Proteins by Anthony R. Means, P. Michael Conn (Eds.)
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