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Query: UMLS:C0272170 (SDS)
 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The resonance Raman spectra and the structures of the heme moiety of Rhodospirillum rubrum cytochrome c' were investigated for its five states characterized by absorption spectra; Types-a and -n of the reduced form and Types-I, -II, and -III of the oxidized form. The frequency of the ligand-sensitive Raman line suggested the coordination of lysine (Nepsilon) at the sixth position of the heme iron of Type-n. The sixth ligand of Type-III was deduced to be either lysine or histidine but would not be methionine. Type-a and Type-II gave the Raman spectra of rather normal high spin type but Type-I was unusual in the sense that the frequencies of the Raman lines associated primarily with methine-bridge CC-stretching vibrations were relatively high in comparison with those of other high spin hemoproteins. Type-I was converted directly to Type-III upon the addition of SDS or 2-propanol but the conversion occurred via Type-II when pH was increased. Structural difference between the high spin hemes of Type-I and Type-II was discussed in detail.
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PMID:Resonance Raman study of the pH-dependent and detergent-induced structural alterations in the heme moiety of Rhodospirillum rubrum cytochrome c'. 2 Sep 77

A basic protein has been purified from sheep brain. The purified protein sedimented in the analytical centrifuge at 56,000 r.p.m. as an homogenous product. This protein induced an allergic encephalitis when injected into guinea pigs. Some physiochemical properties of the protein were studied: the sedimentation coefficient was 1.52 and the molecular weight was 20,000 +/- 2,000, as estimated by electrophoresis in acrylamide gels containing SDS and urea; the specific extinction coefficient (see article) was 6.01 +/- 0.20. The aminoacid composition of the molecule was determined and its most prominent aspects are a high content of arginine and lysine, the presence of a single tryptophan, the total absence of cysteine and cystine and a blocked N-terminal residue. All these properties are very close to those of human and bovine encephalitogenic proteins.
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PMID:Isolation and characterization of a basic encephalitogenic protein from the central nervous system of sheep. 4 99

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.
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PMID:Interaction of the myelin basic protein with the anionic detergent sodium dodecyl sulphate. 7 28

Myosin purified from the abdominal flexor muscle of the lobster, Homarus americanus, has a number average length of 1559 +/- 218 A, a rod like tail 1335 A long and a globular head 225 X 45 A as determined from electron microscopic observations on platinum shadowed preparations. The mass of the molecule was determined to be ca. 486,000 daltons from high speed equilibrium centrifugation studies at neutral and alkaline pH, and by SDS-acrylamide gel electrophoresis. Both sedimentation equilibrium centrifuge studies at alkaline pH and SDS-acrylamide gel electrophoresis experiments, indicate that the molecule contains a heavy chain core (two polypeptide chains weighing ca. 210,000 daltons each) and ca. four light chains of two weight classes (ca. 16,000 and 20,000 daltons). The amino acid composition of the myosin was determined. The specific activities of the Mg2+ -activated, K+/EDTA-activated, and Ca2+ -activated ATPases of the myosin were determined. Kinetic analysis of the digestion of lobster myosin with trypsin suggests that lobster myosin contains three classes of lysine and arginine residues; slowly split (k = 2.07 +/- 0.31 X 10(-2) moles/min2), rapidly split (k = 11.0 +/- 1.83 X 10(-2) moles/min2) and trypsin insensitive. There are 187 +/- 22 slowly split residues, 280 +/- 35 rapidly split residues, and 144 +/- 41 trypsin insensitive bonds per molecule. Comparison of these molecular parameters with those for the vertebrate skeletal muscle myosin indicates that the two myosins are similar in terms of mass, shape and overall polypeptide chain composition but may be considerably different in terms of local polypeptide chain conformation or composition.
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PMID:Comparative studies on the structure and aggregative properties of the myosin molecule. I. The structure of the lobster myosin molecule. 13 6

A lipophilic derivative of neocarzinostatin (NCS), an antitumor antibiotic, was prepared by reaction with a synthetic water-soluble polymer, [(styrene)1 approximately 3-(maleic acid 4 approximately 7/anhydride 1)]. The reaction was carried out at pH 8.6 for 3 h and aimed at modifying the two nonessential amino groups (alpha-amino of Ala-1, epsilon-amino of Lys-20). The NCS-polystyrene (SMANCS) was purified on a column of Sephadex G-100 in 0.05 M ammonium bicarbonate and the main product was obtained as a single peak. The elemental analysis showed an increased C and a decreased N content. U.v. and i.r. absorption spectra for SMANCS showed the presence of styrene. SDS-acrylamide gel electrophoresis at pH 8.5 and the decreased N content suggested a molecular weight of about 25 000, indicating the numbers of polymers conjugated to be about six units, two of which were found attached to the two amino groups. SMANCS was soluble in organic solvents, in contrast to NCS, and in water. SMANCS exhibited increased chemical and biological stability and appeared to possess similar in vitro biological activity.
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PMID:A lipophilic derivative of neocarzinostatin. A polymer conjugation of an antitumor protein antibiotic. 15 71

Explants from rabbit aortic media were incubated in MEM medium supplemented with 14C-lysine and with 10 p. 100 hyperlipemic (type IV and V) or normal human serum respectively. The incubated fragments were extracted at increasing ionic strength. The insoluble collagen and elastin were hydrolysed with collagenase and alcoholic potassium hydroxyde respectively. The radioactivity was determined in the extracts and the radioactive labelling profile of proteins was investigated on polyacrylamide gel electrophoresis in SDS. With the exception of the collagenase extract (polymeric collagen) the incorporation of the radioactivity into insoluble collagen is not altered or increases. These the incubation was carried out in the presence of hyperlipemic serum. Incorporation of the radioactivity into insoluble collagen seems not to be altered. These results show a decreased protein synthesis with a relative increase in the biosynthesis of polymeric insoluble collagen in the aortic media incubated in the presence of hyperlipemic serum.
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PMID:Action of human hyperlipemic sera on the biosynthesis of intercellular matrix macromolecules in aorta organ cultures. 18 73

1. The chemical composition of chromatins obtained from Buffalo rat liver and Morris hepatoma strain 5123 was investigated. 2. The presence of an additional subfraction within the very lysine-rich histone (fl) was states in both kinds of tissues. It amounted to about 8% and 5% of fl in rat liver and Morris hepatoma, respectively. 3. Nuclear phosphoproteins (phenol-soluble) from normal and tumour tissues in polyacrylamide gel in SDS showed some qualitative differences in the range of molecular weights of about 40 000 - 70 000 and over 100 000 daltons.
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PMID:Studies on histones and nuclear phosphoproteins of rat liver and Morris hepatoma. 18 36

For fluorescence labelling intact cells and isolated cell envelopes (membranes) from Salmonella typhimurium and Acholeplasma laidlawii were treated with mixed dansylchloride-lecithin-cholesterol vesicles. This kind of dansylation, which has been supposed to be specific for cell surface proteins, produced fluorescent protein pattern after SDS-polyacrylamide gel electrophoresis only when isolated envelopes were dansylated. Acid hydrolysis of fluorescent cell envelopes of Salmonella typhimurium yielded O-dansyltryosine and epsilon-N-dansyl-lysine besides the free sulfonic acid and unidentified compounds. However, no fluorescent proteins were detectable in cell envelopes isolated from dansylated intact bacteria from Salmonella typhimurium. In accord Acholeplasma laidlawii showed only fluorescence from proteins with a molecular weight higher than 100000.
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PMID:Differential fluorescence labelling with 5-dimethyl-aminonaphthalene-1-sulfonyl chloride of intact cells and isolated membranes in Salmonella typhimurium and Acholeplasma laidlawii. 23 45

This study describes the purification and preliminary characterization of a 94 000 molecular weight protein (S-94) previously known only as a major band in SDS-polyacrylamide gels of total proteins from cultured murine cells. Native S-94 is a soluble constituent of the cytoplasm and sediments at 5.0 S in sucrose gradients, behavior compatible with that of a 94 000 molecular weight monomer. S-94 is purified more than 20-fold from the 100 000 X g supernatant of murine L or L1210 lymphoma cells by DEAE-Sephadex (A-50) chromatography in the presence of 2-mercaptoethanol followed by Sephadex G-200 chromatography in 8 M urea. The protein prepared by this procedure is extensively aggregated, but is essentially homogeneous by SDS-polyacrylamide gel electrophoresis. S-94 preparations from the two types of murine cells behave identically during the purification procedure and are presumed to be the same protein. It appears that these cells contain only one major protein of 94 000 molecular weight. Purified S-94 yields a distinctive pattern of fragments following CNBr degradation, including one peptide of 36 100 molecular weight. The amino acid composition is distinguished by being relatively rich in threonine, glycine and lysine, but poor in valine, leucine and tyrosine.
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PMID:Purification and characterization of a major component from the cytoplasmic matrix of cultured murine L cells. 45 59

Dialdehyde starch (DAS) reacts unspecifically with the amino acid residues of the 11 S globulin from sunflower seed. The modification of the protein causes a decrease of the content of each amino acid. Their blocking reaches maximum values at high pH levels (9,5) and high concentration of protein (5%). Especially high reactivity is shown by arginine as well as by the hydrophobic amino acids isoleucine, valine, and proline, and furthermore by histidine, lysine, asparagine (aspartic acid), and glutamine (glutamic acid). By reaction with DAS at pH 8.0 70% of the amino groups are blocked within 6 h; on the contrary, glyoxale blocks only 30% of the amino groups. Owing to the blockage of charged amino acid groups, a shift of the isoelectric point of the protein to a lower pH (4,3-4,4) takes place; this effect can be followed for 2 days. As a result of the reaction with DAS, only small amounts (10-15%) of intermolecular crosslinkage products with sedimentation coefficients of 17 S and greater than 17 S were formed. But by means of SDS-gel electrophoresis, dimers and trimers of the polypeptide chains in the protein were detected.
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PMID:[Chemical modification of proteins. 5. Modification of the 11-S-globulin from sunflower seed by reaction with dialdehyde starch]. 47 Oct 38


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