Disk electrophoretic study of human preceruloplasmin proteins

Disk acrylamide electrophoresis of plasma from 319 individuals revealed 8–12 protein bands between ceruloplasmin and albumin. Alpha-1-antitrypsin, Gc-globulin, and perhaps alpha-1-lipoprotein were localized in this region with specific antisera. At least nine additional proteins were observed by comparison of the hereditary patterns, differential staining, enzymatic activity, and the alcohol fractionation of these bands. The fractionation data suggest that the protein heterogeneity of this region may be more extensive than that demonstrated by disk acrylamide electrophoresis alone.     

Comparative electrophoretic study on ribosomal proteins from algae

The proteins from cytoplasmic ribosomal subunits of eight species of algae were analyzed by two-dimensional gel electrophoresis. The molecular weights of the proteins were in the range of 10,000 to 55,000. We have compared the protein patterns from the ribosomal subunits of the different species to those of Chlamydomonas reinhardii. It was quite clear that there are many similarities in the protein patterns of all the investigated species. We found for Chlamydomonas eugametos 48, Chlamydomonas noctigama 42, Chlorogonium elongatum 47, Scenedesmus obliquus 40, Chlorella fusca 35, and Euglena gracilis 35 proteins which were homologous to those of Chlamydomonas reinhardii. For the colorless flagellate Polytoma papillatum, we detected 45 proteins homologous to Chlamydomonas reinhardii, so that the generally assumed close relationship between Chlamydomonas and Polytoma is confirmed.     

A disc electrophoretic study of proteins of blue-green algae

Proteins extracted from twenty-one cultures representing fourteen strains of blue-green algae were subjected to disc electrophoresis. Phycocyanin was visible on gels of all species and phycoerythrin on gels of seven species. All extracts gave substantially similar protein patterns although minor differences separate Microcystis aeruginosa, Chlorogloea fritschii, and especially Anacystis nidulans, both from each other and from the other species examined. A set of three protein bands was absent from cultures grown on a medium free of combined nitrogen, but present on similar cultures receiving such additions. However, the bands were also absent from two cultures grown with a combined nitrogen source when incubated at a relatively low light intensity.     

Quantitation of electrophoretic eluted proteins

Quantitation of stained, electroeluted proteins by the classical Lowry and Bradford protein assay is not possible because of some different interferences. In particular we have found that the substance interfering in the Lowry method cannot be removed by trichloroacetic acid precipitation nor can be compensated for by the appropriate blank. Interferences in the Bradford protein assay are due to detergents and pH of the protein buffer as well as to Coomassie brilliant blue R250 electroeluted with the protein sample. However, while these interferences can be compensated for by appropriate blank and standard curves, others (probably due to acrylamide fines) cannot be corrected. All these problems can be overcome by concentration and dialysis of electroeluted samples which permit the removal of interfering substances and the use of Bradford and Lowry protein assay in the 1-20 micrograms range, respectively. Successful applications are described for electroeluted bovine serum albumin, human hexokinase and phosphoglucomutase.     

Comparative electrophoretic study on proteins from mitochondrial and cytoplasmic ribosomes of Saccharomyces cerevisiae

By sodium dodecyl sulfate-acrylamide gel electrophoresis, proteinsof yeast mitochondrial ribosome were shown to be different fromthose of the cytoplasmic counterpart. Fourteen bands found withmitochondrial ribosome did not show any correspondence withthose of the cytoplasmic type. Further, relative amounts ofproteins with their molecular weight more than 50,000 were muchgreater in mitochondrial ribosome, while proteins with theirmolecular weight less than 27,000 were abundant in cytoplasmictype. (Received January 16, 1975; )     

Infrared spectroscopic study of the metal-coordination structures of calcium-binding proteins

Carboxylate (COO⁻) groups can coordinate to metal ions in of the following four modes: ‘unidentate’, ‘bidentate’, ‘bridging’ and ‘pseudo-bridging’ modes. COO⁻ stretching frequencies provide information about the coordination modes of COO⁻ groups to metal ions. We review the Fourier-transform infrared spectroscopy (FTIR) of side-chain COO⁻ groups of Ca²⁺-binding proteins: pike parvalbumin pI 4.10, bovine calmodulin and Akazara scallop troponin C. FTIR spectroscopy of Akazara scallop troponin C has demonstrated that the coordination structure of Mg²⁺ is distinctly different from that of Ca²⁺ in the Ca²⁺-binding site. The assignments of the COO⁻ antisymmetric stretch have been ensured on the basis of the spectra of calcium-binding peptide analogues. The downshift of the COO⁻ antisymmetric stretching mode from 1565 cm^-1 to 1555-1540 cm⁻¹ upon Ca²⁺ binding is a commonly observed feature of FTIR spectra for EF-hand proteins.     

Computation of the electrophoretic mobility of proteins.

A scheme is presented for computing the electrophoretic mobility of proteins in free solution, accounting for the details of the protein shape and charge distribution. The method of Teubner is implemented using a boundary integral formulation within which the velocity distribution, the equilibrium electrical potential around the molecule, and the potential distribution due to the applied field are solved for numerically using the boundary element method. Good agreement of the numerical result is obtained for spheres with the corresponding semi-analytical specialization of Henry's analysis. For protein systems, the method is applied to lysozyme and ribonuclease A. In both cases, the predicted mobility tensors are fairly isotropic, with the resulting scalar mobilities being significantly smaller than for spheres of equal volume and net charge. Comparisons with previously published experimental results for ribonuclease show agreement to be excellent in the presence of a net charge, but poorer at the point of zero charge. The approach may be useful for evaluating approximate methods for estimating protein electrophoretic mobilities and for using electrophoretic measurements to obtain insight into charge distributions on proteins.     

Biosystematic study of mice of the genus Mus: karyotype and electrophoretic analysis of total proteins

Two forms of sympatric mice are captured in North - Tunisia: long - tailed mouse and short - tailed mouse. They are often considered as two semi - species of genus Mus, respectively Mus musculus musculus et Mus musculus spretus. They have the same Karyotype (2n = acrocentrics). The electrophoretic study of total proteins, shows up genetics differences. These two forms of mice may be considered as two different species, as like as mices of Europe: Mus musculus at long-tailed and Mus spretus at short tailed.