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At least 19 recordsLinked to original sources
PubMed1978

Anomalous behavior of the major avian myeloblastosis virus glycoprotein in the presence of sodium dodecyl sulfate.

The sodium dodecyl sulfate (SDS) complex of the major glycoprotein of avian myeloblastosis virus exhibited an anomalously low free electrophoretic mobility compared with those of non-glycosylated protein standards. The apparent molecular weight of the glycoprotein calculated from the relation between log molecular weight and electrophoretic mobility depended on the acrylamide concentration and reached a lower limit of 80,000. The molecular weight was also estimated from the retardation coefficients of protein standards and the viral glycoprotein. This method yielded a molecular weight of 64,000 for the avian myeloblastosis virus glycoprotein. When gel chromatography in SDS was used to determine the apparent molecular weight of the glycoprotein from its hydrodynamic properties alone, the estimated value was 50,000. The generally assigned value of 80,000 daltons for the avian myeloblastosis virus major glycoprotein, as determined by SDS electrophoresis, may be an overestimate due to its relatively low free electrophoretic mobility and peculiar conformation in SDS.

Avian Leukosis Virus↗
PubMed1979

Physical properties of collagen--sodium dodecyl sulfate complexes.

Sodium dodecyl sulfate (NaDodSO4)--polyacrylamide gel electrophoresis and gel filtration chromatography of protein--NaDodSO4 complexes are frequently used to characterize collagen-like polypeptide components in mixtures obtained from extracts of basement membranes. However, electrophoresis yields anomalously high apparent molecular weights for collagenous polypeptides when typical globular proteins are used as molecular weight standards, and the use of gel filtration chromatography for this purpose was suspect because Nozaki et al. [Nozaki, Y., Schechter, N. M., Reynolds, J. A., & Tanford, C. (1976) Biochemistry 15, 3884--3890] found that asymmetric particles, including NaDodSO4--protein complexes, coeluted with native globular proteins of lower Stokes radius, when Sepharose 4B was used. To understand these effects and to improve the characterization of collagenous polypeptides, we investigated the secondary structure of NaDodSO4--collagen complexes with the use of circular dichroism, measured the NaDodSO4 content, studied the dependence of electrophoretic mobility on gel concentration, and extended work on gel filtration by use of a more porous gel, Sepharose CL-4B. We found that the anomalous behavior of collagen chains on NaDodSO4--polyacrylamide gel electrophoresis is due in large part to treatment of data and that the method can be used to determine rather accurate values for the number of residues per polypeptide chain. Our gel filtration results indicated that reliable molecular weights can be obtained when Sepharose CL-4B is used. These methods can be applied equally well to collagenous and noncollagenous polypeptides.

Animals↗
PubMed1978

Changes in the state of ionization of carboxyl groups in elastin in response to the binding of sodium dodecyl sulfate.

The interaction of sodium dodecyl sulfate with elastin has been studied by complexometric titration. Approximately 1.2 mumoles of protons with a pKapp of 5.45 are taken up by 10 milligrams of insoluble elastin upon the binding of detergent, apparently due to the protonation of normally ionized carboxylate functions in this protein. Since ionized carboxylate functions of elastin are essential for its interaction with elastase and, possibly, metallic cations, these results may have physiological significance in view of the affinity of elastin for lipid-like ligands.

Chemical Phenomena↗
PubMed1978

A calorimetric comparison of the interaction of sodium dodecyl sulfate with cytochrome c and erythrocyte glycoproteins.

The interactions of sodium dodecyl sulfate with cytochrome c and erythrocyte glycoproteins have been studied by the method of titration calorimetry. It was found that the initial addition of sodium dodecyl sulfate to cytochrome c caused an endothermic unfolding of the protein, detectable by circular dichroism (CD). This was followed by the exothermic binding of sodium dodecyl sulfate to the protein, without further CD-detectable conformational changes. In contrast, sodium dodecyl sulfate bound directly to the erythrocyte glycoproteins in an exothermic reaction without any accompanying CD-detectable conformation changes. This indicates that the glycoproteins solubilized in aqueous media have exposed hydrophobic regions which can interact directly with this detergent. The enthalpy changes and stoichiometries of binding are reported.

Calorimetry↗
PubMedDate not supplied

[Effect of sodium dodecyl sulfate on biological membranes].

Effect of sodium dodecyl sulfate (SDS) on yeast cells resulting in the cellular proteins release from the cells was examined. The influence of pH, ionic strength, the agent concentration and the cells lipids content on the proteins extraction degree was studied. It is assumed that the proteins release is due to the plasma membrane solubilization under the surfactant treatment. It is established that the mechanism of the monimer--membrane interaction and that of the micelle--membrane interaction are likely to be different. It is shown that micelle-like surfactant--protein complexes can solubilize the membrane as well as the SDS micellies. It is found an increase of the ionic strength decreases the efficiency of the SDS action probably due to an increase of the micelle volume. It is assumed that the efficiency of the SDS action on the cell is limited particularly by the ratio of cell wall pere size to the size of micelles formed by the agent in the solution. It is shown also that removal of the largest portion of the lipids from the yeast cell favours an increase in the efficiency of the SDS extractive action at the agent concentrations larger than the critical micelle concentration value probably due to the corresponding decrease of the amount of the cellular components which must be solubilized by the surfactant micelles.

Chemical Phenomena↗
PubMed1979

Charge separation of proteins complexed with sodium dodecyl sulfate by acid gel electrophoresis in the presence of cetyltrimethylammonium bromide.

Globular proteins, casein, and membrane proteins which were reacted with sodium dodecyl sulfate were studied by acid urea gel electrophoresis. The sodium dodecyl sulfate bound tightly to the proteins, producing a more acidic charge which prevented migration into the gel. When cetyltrimethylammonium bromide was added to the sodium dodecyl sulfate-protein complexes, the sodium dodecyl sulfate apparently reacted with cetyltrimethylammonium bromide and dissociated so that the proteins migrated in acid gel in a normal manner as compared to the proteins without any added detergent. The sodium dodecyl sulfate-cetyltrimethylammonium bromide complex could be removed from the proteins by centrifugation. Thus, cetyltrimethylammonium bromide used in conjunction with acid gel electrophoresis allows direct comparison by charge of proteins fractionated in the presence of sodium dodecyl sulfate with the starting mixture of proteins not exposed to detergent. The reaction of cetyltrimethylammonium bromide with sodium dodecyl sulfate in acidic urea also provides a simple convenient method of removal of sodium dodecyl sulfate from proteins.

Cetrimonium Compounds↗
PubMed1976

The solution behavior of the bovine myelin basic protein in the presence of anionic ligands. Binding behavior with the red component of trypan blue and sodium dodecyl sulfate.

The interaction of the azo dye (2,3'-dimethyldiphenyl-7-azo-8-amino-1-napthol 3,6-disulfonic acid (TBR) and sodium dodecyl sulfate with the bovine myelin basic protein has been studied using absorbance, circular dichroism and 220 MHz PMR spectroscopy. Additional analyses of the binding reaction were carried out using light scattering, ultracentrifugal and electrophoretic techniques. A procedure for preparing pure TBR was developed. A modified structure for this synthesized TBR has been suggested. The mechanism of TBR binding to the myelin basic protein was found to be metachromatic. In addition, the interaction of TBR with the basic protein which gives rise to aggregation of the dye bound species was found to be analogous to the model proposed by Schwarz, G. and Seelig-Löffler, A. ((1975) Biochim. Biophys. Acta 379, 125-138) to explain the binding of acridine orange with poly (alpha-L-glutamic acid). PMR spectral analyses suggested that arginine residues provide the majority of primary sites of attachment on the basic protein for TBR. The effect of sodium dodecyl sulfate binding with the bovine myelin basic protein was found to induce a minimal change in the conformation of the protein. The induction of only about 20% alpha helial structure could be demonstrated and the binding was reversed by raising the solution temperature to 73 degrees C. The difference in the observed behavior of basic protein arising from TBR binding as opposed to the binding of sodium dodecyl sulfate is viewed as resulting from two different binding mechanisms. The binding behavior of TBR is primarily a consequence of charge-charge interaction while the binding effects of sodium dodecyl sulfate are a consequence of hydrophobic interaction. The sodium dodecyl sulfate binding acts as a shield which limits charge-charge interaction in the basic protein molecule thus preventing aggregate formation while TBR imposes no such restraints.

Animals↗
PubMed1977

Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.

A rapid and convenient method for peptide mapping of proteins has been developed. The technique, which is especially suitable for analysis of proteins that have been isolated from gels containg sodium dodecyl sulfate, involves partial enzymatic proteolysis in the presence of sodium dodecyl sulfate and analysis of the cleavage products by polyacrylamide gel electrophoresis. The pattern of peptide fragments produced is characteristic of the protein substrate and the proteolytic enzyme and is highly reproducible. Several common proteases have been used including chymotrypsin, Staphylococcus aureus protease, and papain.

Alkaline Phosphatase↗
PubMed1978

Removal of unbound sodium dodecyl sulfate (SDS) from proteins in solution by electrophoresis through triton x-100-agarose.

Residual sodium dodecyl sulfate (SDS) introduces artifacts into immuno- and counterimmunoelectrophoretic analysis of proteins which have been eluted from preparative SDS-polyacrylamide gels. Unbound SDS can be removed by electrophoretic passage of eluted solutions through a barrier of Triton X-100 in agarose in which the anionic and non-ionic detergents interact to form micelles.

Counterimmunoelectrophoresis↗
PubMed1979

Thermodynamic analysis of the nonspecific interaction of sodium dodecyl sulfate with swollen Bio-Gel beads.

In frontal gel chromatography on Bio-Gel P-2, sodium dodecyl sulfate (SDS) at the concentrations below its critical micelle concentration (cmc) showed anomalously high partition coefficients (Kav obs) indicative of strong interactions with the swollen gel phase; further, Kav obs was found to increase with concentration and temperature. This preferential partition of SDS in the Bio-Gel phase was analyzed in terms of the transfer free energy of SDS from the mobile phase (0.1 M NaCl) to the swollen Bio-Gel phase. The results showed that the overall transfer process is primarily governed by hydrophobic free energy arising from the anomalous nature of hydrated water in the gel matrix; that is, in highly hydrated water "iceberg" formation is evidently limited and the hydrophobic free energy is accordingly lowered, resulting in the preferential partition of SDS in the swollen Bio-Gel phase. The increase in the negativity of transfer free energy with concentration, though relatively small, indicated a definite tendency for the formation of SDS clusters in the gel phase. Finally, a model illustrating the states of SDS molecules in the gel matrix is presented, which may also be pertinent to SDS-protein and SDS-amylose complexes.

Chromatography, Gel↗
PubMed1976

Stepwise degradation of serum low denisty lipoprotein by sodium dodecyl sulfate.

The structure of human serum low density lipoprotein (LDL) was investigated by perturbing the LDL structure with sodium dodecyl sulfate (SDS). The change in LDL structure induced by the addition of SDS was monitored by sedimentation velocity measurements, ultraviolet difference spectroscopy, fluorescence spectroscopy and proteolytic digestion of apo-LDL with subtilisin BPN' [EC 3.4.21.14]. As the concentration of SDS was increased from 0.1 mg/ml to 3 mg/ml with LDL concentrations between 2.0 mg/ml and 4.4 mg/ml, the sedimentation coefficient of LDL changed in three distinct steps. It was found by chemical analyses that not more than 30% of the total lipid was lost from LDL in the second step, whereas the final step in the change of sedimentation coefficient corresponded to the complete removal of apo-LDL from the constituent lipids of LDL. The ultraviolet difference spectrum between the native and SDS-treated LDL and the quenching of LDL fluorescence underwent about 80% of the total change while the SDS concentration was only sufficient to cause the second of the three step changes in sedimentation coefficient. SDS-polyacrylamide gel electrophoresis of apo-LDL treated with subtilisin BPN' also showed that more than 70% of apo-LDL became susceptible to proteolysis under the same conditions. These results were interpreted as indicating that the solubilization of 20 to 30% of the lipids on the surface of LDL exposed nearly 80% or more of apo-LDL to the solvent. A small portion of apo-LDL was, however, still firmly anchored to the remaining lipid micelle as long as the concentration of SDS was less than that required to cause the final step of the change in sedimentation coefficient.

Animals↗
PubMed1979

A new method for the measurement of lipoprotein lipase in postheparin plasma using sodium dodecyl sulfate for the inactivation of hepatic triglyceride lipase.

Lipoprotein lipase (LPL) and hepatic triglyceride lipase (H-TGL) are lipolytic activities found in postheparin plasma. A simple and precise method for the direct determination of LPL in postheparin plasma is described. Pre-incubations of this plasma (45--60 min at 26 degrees C) with sodium dodecyl sulfate (35--50 mM) in 0.2 M Tris-HCl buffer, pH 8.2, results in the inactivation of H-TGL, while leaving LPL fully active. Direct determination of H-TGL is done in a separate aliquot of the same postheparin plasma sample using previously reported assay conditons that do not measure LPL. The sodium dodecyl sulfate-resistant lipolytic activity has the characteristics of LPL as judged by a) its activation by serum and by apolipoprotein C-II; b) its inactivation (over 90%) by 0.75 M NaCl; and c) its inactivation by a specific antiserum. No sodium dodecyl sulfate-resistant activity was found in postheparin plasma from a patient with LPL deficiency (primary type I hyperlipoproteinemia). An excellent correlation of values was obtained (r = 0.99) for 30 samples assayed after sodium dodecyl sulfate treatment and after immuno-inactivation of H-TGL. The intra-assay coefficient of variation was +/- 11% and 4% before and after normalization of values, respectively.

Female↗
PubMed1978

Determination of total and direct bilirubins in serum with sodium dodecyl sulfate as an accelerator.

A new method for the determination of total and conjugated bilirubins in serum with use of sodium dodecyl sulfate (SDS) is described. In the presence of SDS, the reaction of bilirubin with diazotized sulfanilic acid proceeded smoothly and was completed within 15 min at room temperature, thus resulting in a clear solution having a maximal absorbance at 565 nm which was linear up to a level of 200 mg/l bilirubin concentration. The advantages of this method are: (1) a clear reaction mixture results in any case; (2) the result is not affected by hemolysis, lipemic and turbid sera. The proposed method offers a new general application for the measurement of total and conjugated bilirubins in serum.

Ascorbic Acid↗
PubMed1978

Self-association of human erythrocyte glycophorin A. Appearance of low mobility bands on sodium dodecyl sulfate gels.

We have examined the self-association of glycophorin A, the major sialoglycoprotein of the human erythrocyte membrane, using sodium dodecyl sulfate (SDS) polyacrylamide gels and circular dichroism. Pure glycophorin A has a tendency to form multiple bands on SDS gels at positions of higher apparent molecular weight than the PAS 1 and PAS 2 bands previously seen. These high molecular weight bands do not have mobilities corresponding to integral polymers of PAS 1 and PAS 2. Circular dichroism spectra of solutions giving rise to these bands or to PAS 1 and PAS 2 bands alone, indicate that these species all have essentially the same peptide conformation.

Circular Dichroism↗
PubMed1975

A study of protein-sodium dodecyl sulfate complexes by transient electric birefringence.

The method of transient electric birefringence has been applied to study the conformation of protein-sodium dodecyl sulfate complexes. A model of a deformable prolate ellipsoid has been proposed for the protein-dodecyl sulfate complex. This model is compared to the models proposed by J. A. Reynolds and C. Tanford (1970), J. Biol. Chem. 245, 5161) and K. Shirahama, K. Tsujii, and T. Takagi (1974, J. Biochem. 75, 309). Differences between these latter two models are resolved by the model presented here. In addition, it has been demonstrated that protein molecular weights may be obtained from the slow relaxation time for transient electric birefringence of protein-dodecyl sulfate complexes.

Animals↗
PubMed1977

[Electrophoretic patterns of differently prepared fibrinogen subunits in sodium dodecyl sulfate containing polyacrylamide gels].

The electrophoretic behaviour of mercapto, carboxamidomethyl, carboxymethyl and thiosulfonic acid derivatives of rabbit fibrinogen subunits was investigated electrophoretically in sodium dodecyl sulfate containing polyacrylamide gels. Comparing carboxymethyl, carboxamidomethyl and thiosulfonic acid derivatives with the corresponding mercapto subunits divergent electrophoretic patterns were observed. Especially, the position of the Bbeta-chain was strongly dependent on the method of preparation. Similar results were obtained from investigating electrophoretic mobilities of albumin with differently substituted SH-groups after reduction with mercaptoethanol.

Albumins↗
PubMed1977

Immunological identification of complex proteins resolved by sodium dodecyl sulfate polyacrylamide disc gel electrophoresis.

Immunological identification of an antigen resolved from a protein complex by sodium dodecyl sulfate polyacrylamide gel electrophoresis has been attained. The identification is based on the formation of immunoprecipitin lines after the antigen diffuses laterally from acrylamide gel transverse slices into a surrounding agarose gel. This technique was designed for study of contractile and regulatory protein complexes of non-muscle cells where the scarcity of tissue precludes easy purification or high yield of muscle-like proteins. It complements double-gel immunodiffusion or immunoelectrophoresis and its use may be extended to other protein complexes.

Actinin↗