scholarly journals Interaction of the myelin basic protein with the anionic detergent sodium dodecyl sulphate

1978 ◽  
Vol 169 (2) ◽  
pp. 281-285 ◽  
Author(s):  
A J S Jones ◽  
M G Rumsby
Keyword(s):  
Myelin Basic Protein ◽  
Sodium Dodecyl Sulphate ◽  
Basic Protein ◽  
Hydrophobic Interactions ◽  
Rapid Development ◽  
Sodium Dodecyl ◽  
Molecular Size ◽  
Transient Increase ◽  
Tryptophan Residue ◽  
Molar Ratios

The interaction of the myelin basic protein and two peptides derived from it with the anionic detergent SDS (sodium dodecyl sulphate) was studied. At molar ratios of detergent/protein of up to approx. 20:1 the transient increase in turbidity (as measured by increases in A230) is proportional to the ratio. Between ratios of 30:1 and 100:1 the effect of the detergent is constant and maximal. At molar ratios exceeding 100:1 the transient increase in turbidity decreases with increasing amounts of detergent. With increasing ionic strength the rapid development of turbidity is inhibited, whereas the slow decay of turbidity is not affected. Neither of the peptide fragments produced by cleavage of the myelin basic protein at the single tryptophan residue, nor both when mixed, produce measurable turbidity when mixed with SDS. Under similar conditions poly-L-lysine of similar molecular size to the basic protein shows the increase in turbidity but not the decay. The interaction between the protein and SDS is interpreted in molecular terms, which involve the initial ionic interaction of the detergent with protein resulting in aggregation and turbidity in the solution. Within the aggregated complexes molecules rearrange to maximize hydrophobic interactions.

scholarly journals Characterization of proteins from the cytoskeleton of Giardia lamblia

1983 ◽  
Vol 59 (1) ◽  
pp. 81-103 ◽  
Author(s):  
R. Crossley ◽  
D.V. Holberton
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulphate ◽  
Giardia Lamblia ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Molecular Size ◽  
Molecular Weights

Proteins from the axonemes and disc cytoskeleton of Giardia lamblia have been examined by sodium dodecyl sulphate/polyacrylamide gel electrophoresis. In addition to tubulin and the 30 X 10(3) molecular weight disc protein, at least 18 minor components copurify with the two major proteins in Triton-insoluble structures. The most prominent minor bands have the apparent molecular weights of 110 X 10(3), 95 X 10(3) and 81 X 10(3). Protein of 30 X 10(3) molecular weight accounts for about 20% of organelle protein on gels. In continuous 25 mM-Tris-glycine buffer it migrates mostly as a close-spaced doublet of polypeptides, which are here given the name giardins. Giardia tubulin and giardin have been purified by gel filtration chromatography in the presence of sodium dodecyl sulphate. Well-separated fractions were obtained that could be further characterized. Both proteins are heterogeneous when examined by isoelectric focusing. Five tubulin chains were detected by PAGE Blue 83 dye-binding after focusing in a broad-range ampholyte gel. Giardin is slightly less acidic than tubulin. On gels it splits into four major and four minor chains with isoelectric points in the pI range from 5.8 to 6.2. The amino acid composition of the giardin fraction has been determined, and compared to Giardia tubulin and a rat brain tubulin standard. Giardins are rich in helix-forming residues, particularly leucine. They have a low content of proline and glycine; therefore they may have extensive alpha-helical regions and be rod-shaped. As integral proteins of disc microribbons, giardins in vivo associate closely with tubulin. The properties of giardins indicate that in a number of respects - molecular size, charge, stoichiometry - their structural interaction with tubulin assemblies will be different from other tubulin-accessory protein copolymers studied in vitro.

scholarly journals The molecular size of N-methylglutamate dehydrogenase of Pseudomonas aminovorans

1977 ◽  
Vol 167 (2) ◽  
pp. 509-512 ◽  
Author(s):  
C W Bamforth ◽  
P J Large
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein A ◽  
Sodium Dodecyl ◽  
Molecular Size ◽  
Partial Specific Volume ◽  
Triton X

N-Methylglutamate dehydrogenase, purified to a specific activity of 0.29 unit/mg of protein, gave one band on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, corresponding to a molecular weight of 130 000. Enzyme-Triton complexes were found to have a partial specific volume of 0.73 cm3/g, suggesting that the protein binds less than 0.1 g of Triton/g of protein. A molecular weight for the intact enzyme in the presence of 1% (w/v) Triton X-100 of 550 000 suggested that the enzyme may be a tetramer.

scholarly journals Collagen fibril formation in the presence of sodium dodecyl sulphate

1985 ◽  
Vol 228 (3) ◽  
pp. 551-556 ◽  
Author(s):  
G W Dombi ◽  
H B Halsall
Keyword(s):  
Conformational Changes ◽  
Sodium Dodecyl Sulphate ◽  
Collagen Fibril ◽  
Hydrophobic Interactions ◽  
Sodium Dodecyl ◽  
Distal Region ◽  
Fibril Formation ◽  
Collagen Fibrillogenesis ◽  
Fibril Morphology

Sodium dodecyl sulphate (SDS) was used to weaken both the electrostatic and the hydrophobic interactions during collagen fibrillogenesis in vitro. The rate and extent of fibril formation as well as fibril morphology were affected by SDS concentration. Both the formation of large fibrils at 0.3 mM-SDS and the complete cessation of fibril formation at 0.5 mM-SDS were considered to be the result of SDS-induced conformational changes in the non-helical telopeptides. A possible mechanism of SDS interaction with the N-terminal and the distal region of the C-terminal telopeptides is offered.

Isolation and characterization of calcineurin from bovine brain

1985 ◽  
Vol 63 (8) ◽  
pp. 1000-1006 ◽  
Author(s):  
Ramesh C. Gupta ◽  
Ramji L. Khandelwal ◽  
Prakash V. Sulakhe
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Myelin Basic Protein ◽  
Phosphatase Activity ◽  
Inhibitory Activity ◽  
Gel Electrophoresis ◽  
Basic Protein ◽  
Sodium Dodecyl ◽  
Subunit A ◽  
Isolation And Characterization ◽  
Dodecyl Sulfate

Calcineurin was isolated from bovine cerebrum extracts by sequential chromatography on Affi-Gel blue and calmodulin affinity columns. Calcineurin so isolated was ~90% pure and was composed of equimolar amounts of subunit A (Mr = 61 000 – 63 000) and subunit B (Mr = 15 000 – 17 000) when examined by sodium dodecyl sulfate gel electrophoresis. A polypeptide (<10%) with Mr = 71 000 whose function and role remains to be investigated, was routinely detected in the calcineurin preparation. Both inhibitory activity (towards calmodulin-dependent cAMP phosphodiesterase) and phosphatase activity (with 32P-labelled myelin basic protein as substrate) were associated with calcineurin as evidenced by (i) coelution from Affi-Gel blue, Affi-Gel calmodulin, diethythaminoethyl-Sepharose, and Sephacryl S-200 chromatography columns; (ii) association with the same protein band on nondenaturing gels; (iii) similar stability upon storage at 4 °C and with repeated freezing and thawing; and (iv) parallel heat inactivation. Phosphatase activity of calcineurin was maximal with 32P-labelled myelin basic protein as the substrate. Using this substrate, enzyme activity was generally stimulated 5- to 10-fold in the presence of Ca2+ and calmodulin; half-maximal activation (A0.5) was observed with 25 nM calmodulin. Calmodulin increased the Vmax of the reaction without affecting the Km for the substrate. Optimum temperature and pH for the reaction were 45 °C and 7, respectively, in both the absence and presence of Ca2+ and calmodulin. The presence of sodium dodecyl sulfate in the assay mixtures caused a decrease in Ca2+ –calmodulin dependent phosphatase but an increase in Mn2+ –calmodulin dependent phosphatase; inhibitory activity was decreased, although to a lesser extent. When A and B subunits of calcineurin were resolved by polyacrylamide gel electrophoresis in the presence of MnCl2 and a low concentration of sodium dodecyl sulfate, the phosphatase activity was found to be associated with subunit A and was stimulated by MnCl2 or MnCl2 + calmodulin.

scholarly journals SDS-Stabilized CuInSe2/ZnS Multinanocomposites Prepared by Mechanochemical Synthesis for Advanced Biomedical Application

Nanomaterials ◽  
2020 ◽  
Vol 11 (1) ◽  
pp. 69
Author(s):  
Erika Dutková ◽  
Zdenka Lukáčová Bujňáková ◽  
Oleh Sphotyuk ◽  
Jana Jakubíková ◽  
Danka Cholujová ◽  
...  
Keyword(s):  
Particle Size ◽  
Mechanochemical Synthesis ◽  
Sodium Dodecyl Sulphate ◽  
Biomedical Application ◽  
Zinc Acetate Dihydrate ◽  
Sodium Dodecyl ◽  
Myeloma Cell ◽  
Planetary Mill ◽  
Molar Ratios ◽  
Multiple Myeloma Cell

The CuInSe2/ZnS multiparticulate nanocomposites were first synthesized employing two-step mechanochemical synthesis. In the first step, tetragonal CuInSe2 crystals prepared from copper, indium and selenium precursors were co-milled with zinc acetate dihydrate and sodium sulfide nonahydrate as precursors for ZnS in different molar ratios by mechanochemical route in a planetary mill. In the second step, the prepared CuInSe2/ZnS nanocrystals were further milled in a circulation mill in sodium dodecyl sulphate (SDS) solution (0.5 wt.%) to stabilize the synthesized nanoparticles. The sodium dodecyl sulphate capped CuInSe2/ZnS 5:0-SDS nanosuspension was shown to be stable for 20 weeks, whereas the CuInSe2/ZnS 4:1-SDS one was stable for about 11 weeks. After sodium dodecyl sulphate capping, unimodal particle size distribution was obtained with particle size medians approaching, respectively, 123 nm and 188 nm for CuInSe2/ZnS 5:0-SDS and CuInSe2/ZnS 4:1-SDS nanocomposites. Successful stabilization of the prepared nanosuspensions due to sodium dodecyl sulphate covering the surface of the nanocomposite particles was confirmed by zeta potential measurements. The prepared CuInSe2/ZnS 5:0-SDS and CuInSe2/ZnS 4:1-SDS nanosuspensions possessed anti-myeloma sensitizing potential assessed by significantly reduced viability of multiple myeloma cell lines, with efficient fluorescence inside viable cells and higher cytotoxic efficacy in CuInSe2/ZnS 4:1-SDS nanosuspension.

Myelin basic protein binds heme at a specific site near the tryptophan residue

Biochemistry ◽  
1987 ◽  
Vol 26 (8) ◽  
pp. 2175-2182 ◽  
Author(s):  
Stephen J. Morris ◽  
Diane Bradley ◽  
Anthony T. Campagnoni ◽  
Gerald L. Stoner
Keyword(s):  
Myelin Basic Protein ◽  
Basic Protein ◽  
Specific Site ◽  
Tryptophan Residue

scholarly journals Phosphorylation in vivo of four basic proteins of rat brain myelin

1982 ◽  
Vol 201 (1) ◽  
pp. 39-47 ◽  
Author(s):  
Harish C. Agrawal ◽  
Keith O'Connell ◽  
Charlotte L. Randle ◽  
Daya Agrawal
Keyword(s):  
Amino Acid ◽  
Rat Brain ◽  
Sodium Dodecyl Sulphate ◽  
Basic Protein ◽  
Sodium Dodecyl ◽  
Amino Acid Sequences ◽  
Intracerebral Injection ◽  
Partial Acid Hydrolysis ◽  
Basic Proteins

When rat brain myelin was examined by sodium dodecyl sulphate/polyacrylamideslab-gel electrophoresis followed by fluorography of the stained gel, it was found that a host of proteins of rat brain myelin were labelled 2, 4 and 24h after the intracerebral injection of H332PO4. Among those labelled were proteins migrating to the positions of myelin-associated glycoprotein, Wolfgram proteins, proteolipid protein, DM-20 and basic proteins. The four basic proteins with mol.wts. 21000, 18000 (large basic protein), 17000 and 14000 (small basic protein) were shown to be phosphorylated after electrophoresis in both acid-urea- and sodium dodecyl sulphate-containing gel systems followed by fluorography. The four basic proteins imparted bluish-green colour, after staining with Amido Black, which is characteristic of myelin basic proteins. The four basic proteins were purified to homogeneity. Fluorography of the purified basic proteins after re-electrophoresis revealed the presence of phosphorylated high-molecular-weight ‘polymers’ associated with each basic protein. The amino acid compositions of the phosphorylated large basic protein and small basic proteins are compatible with the amino acid sequences. Proteins with mol.wts. 21000 and 17000 gave the expected amino acid composition of myelin basic proteins. Radiolabelled phosphoserine and phosphothreonine were identified after partial acid hydrolysis of the four purified basic proteins. The [32P]phosphate–protein bond in the basic protein was stable at an acidic pH but was readily hydrolysed at alkaline pH, as would be expected of phosphoester bonds involving both serine and threonine residues. Double-immunodiffusion analysis demonstrated that the four phosphorylated proteins showed complete homology when diffused against antiserum to a mixture of small and large basic proteins. Since the four basic proteins of rat brain myelin were phosphorylated both in vivo and in vitro it is postulated that the same protein kinase is responsible for their phosphorylation in both conditions.

scholarly journals Localization of sites for ionic interaction with lipid in the C-terminal third of the bovine myelin basic protein

1977 ◽  
Vol 167 (3) ◽  
pp. 583-591 ◽  
Author(s):  
A J S Jones ◽  
M G Rumsby
Keyword(s):  
Myelin Basic Protein ◽  
Basic Protein ◽  
Protein Molecule ◽  
Molar Ratio ◽  
Tryptophan Residue ◽  
Peptide Fragment ◽  
Neutral Complex ◽  
Chloroform Phase ◽  
Complex Lipids ◽  
Soluble Complexes

The myelin basic protein from bovine brain tissue was purified and the two peptides obtained by cleavage of the polypeptide chain at the single tryptophan residue were isolated. The interaction of these peptides and the intact basic protein with complex lipids was investigated by following the solubilization of lipid-protein complexes into chloroform in a biphasic solvent system. The C-terminal peptide fragment (residues 117-170) and the intact basic protein both formed chloroform-soluble complexes with acidic lipids, but not with neutral complex lipids. The N-terminal fragment (residues 1-115) did not form chloroform-soluble complexes with either acidic or neutral complex lipids. The molar ratio of lipid to protein that caused a 50% loss of protein from the upper phase to the lower chloroform phase was the same for the intact basic protein as for the smaller C-terminal peptide fragment. Phosphatidylserine and phosphatidylinositol were approximately twice as efficient as sulphatide at causing protein redistribution to the chloroform phase. The results are interpreted as indicating that the sites for ionic interactions between lipid and charged groups on the basic protein of myelin are located in the C-terminal region of the protein molecule.

scholarly journals Thermodynamic Analysis of Myelin Basic Protein Adsorbed on Liquid Crystalline Dioleoylphosphatidylcholine Monolayer

Scanning ◽  
2019 ◽  
Vol 2019 ◽  
pp. 1-9
Author(s):  
Zhang Lei ◽  
Sun Runguang ◽  
Hao Changchun ◽  
Yang Huihui ◽  
Hu Chengxi
Keyword(s):  
Myelin Basic Protein ◽  
Surface Pressure ◽  
Liquid Crystalline ◽  
Basic Protein ◽  
Hydrophobic Interactions ◽  
Mass Conservation ◽  
Conservation Equation ◽  
Molecular Area ◽  
Unsaturated Lipid ◽  
Mass Conservation Equation

To investigate the stability and dynamic characteristics of monolayer adsorbed on unsaturated lipid dioleoylphosphatidylcholine (DOPC) with varying concentrations of myelin basic protein (MBP), the system is studied by applying Langmuir technique and making atomic force microscope (AFM) observation, which is based on the mass conservation equation analysis method referred to in the thermodynamics theory. As indicated by surface pressure-mean molecular area (π−A) and surface pressure-adsorption time (π−T) isotherms, the physical properties of monolayer derived from the interaction of varying concentrations of MBP with liquid crystalline unsaturated lipid DOPC molecules were qualitatively studied. As revealed by surface morphology analysis with AFM, the micro region was expanded as the concentration of MBP in the subphase was on the increase, suggesting that hydrophobic interactions led to the MBP insertion, thus causing accumulation of the MBP on the surface of the monolayer. Experimental results have demonstrated that the partition coefficient of the interaction between MBP and unsaturated phospholipid DOPC and the molecular area of MBP adsorbed on the monolayer film was calculated using the mass conservation equation. In addition, not only does the varying concentration of MBP in the subphase exerts significant effects on the arrangement and conformation of DOPC monolayer, it also has certain guiding significance to exploring the structural changes to biofilm supramolecular aggregates as well as the pathogenesis and treatment of related diseases.

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