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

Calf lens fiber membranes were photolyzed in the presence and absence of sensitizers and scavengers. Photolytic damage was assessed by SDS-polyacrylamide gel electrophoresis, UV and fluorescence spectra and amino acid analyses. With irradiation, there is an apparent polymerization of the major membrane polypeptide (MP26) and the formation of material which does not enter SDS-polyacrylamide gels. Some degradation was also observed. These changes are accompanied by losses of histidine and tryptophan and changes in the UV spectra. The rate of photolysis is enhanced in the presence of the glucoside of 3-hydroxykynurenine (3-OH-KYN), a compound endogenous to the lens. The reaction is retarded in the presence of sulfhydryl-containing compounds such as glutathione.
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PMID:The photolysis of lens fiber membranes. 402 86

Poly-A RNA extracted from the rat liver was translated in a cell-free wheat germ system and a rabbit reticulocyte lysate. The subunit of tryptophan pyrrolase precipitated by specific antiserum after synthesis in vitro has the same molecular weight as the corresponding subunit derived from the rat liver. With specific antiserum prepared against tyrosine aminotransferase, however, a radioactive protein from both the in vitro assays was precipitated with an about 5% higher molecular weight than the tyrosine aminotransferase subunit precipitated from rat liver. The immunological evidence and the comparison of the specific peptide patterns prepared by cyanogen bromide treatment showed that the in vitro product corresponds to tyrosine aminotransferase. Various concentrations of potassium or spermidine used in the wheat germ translation system did not alter the size of the enzyme subunit synthesized. The run of the tyrosine aminotransferase purified form the rat liver in the SDS-polyacrylamide gel electrophoresis was not influenced by treatment with Escherichia coli alkaline phosphatase. The possibility is discussed that the larger enzyme synthesized in vitro represents a precursor molecule which is cleaved proteolytically in vivo.
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PMID:Translation of poly-A RNA from rat liver in vitro. Evidence for a high molecular weight subunit of tyrosine aminotransferase. 615 19

DNA sequences coding for the immunogenic capsid protein VP1 and/or VP3 of poliovirus strain LSc-2ab (Sabin 1) were prepared by digesting the cloned complementary DNA with restriction endonuclease PstI. The DNA fragments were inserted into the unique PstI site of Escherichia coli plasmid vectors pBR322, pKT 280 and/or pKT 287 that lay in the region expressed under control of the penicillinase promoter system. In the expression vectors, poliovirus sequences were designed to be read in phase and therefore to be expressed as fusion proteins with the bacterial peptides. In addition, the Escherichia coli tryptophan operon promoter-operator system was inserted upstream of the penicillinase system to obtain stronger expression of the poliovirus sequences. Escherichia coli transformed with these plasmids appeared to produce the antigenic polypeptides, which were detected by immunoprecipitation with antibodies to capsid proteins VP1 and/or VP3 followed by SDS-polyacrylamide gel electrophoresis.
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PMID:Expression of poliovirus complementary DNA coding for viral antigenic determinants in Escherichia coli. 620 64

Interaction of N,N'-dicyclohexylcarbodiimide (DCCD) with ATPase of Mycobacterium phlei membranes results in inactivation of ATPase activity. The rate of inactivation of ATPase was pseudo-first order for the initial 30-65% inactivation over a concentration range of 5-50 microM DCCD. The second-order rate constant of the DCCD-ATPase interaction was k = 8.5 X 10(5) M-1 X min(-1). The correlation between the initial binding of [14C]DCCD and 100% inactivation of ATPase activity shows 1.57 nmol DCCD bound per mg membrane protein. The proteolipid subunit of the F0F1-ATPase complex in membranes of M. phlei with which DCCD covalently reacts to inhibit ATPase was isolated by labeling with [14C]DCCD. The proteolipid was purified from the membrane in free and DCCD-modified form by extraction with chloroform/methanol and subsequent chromatography on Sephadex LH-20. The polypeptide was homogeneous on SDS-acrylamide gel electrophoresis and has an apparent molecular weight of 8000. The purified proteolipid contains phosphatidylinositol (67%), phosphatidylethanolamine (18%) and cardiolipin (8%). Amino acid analysis indicates that glycine, alanine and leucine were present in elevated amounts, resulting in a polarity of 27%. Cysteine and tryptophan were lacking. Butanol-extracted proteolipid mediated the translocation of protons across the bilayer, in K+-loaded reconstituted liposomes, in response to a membrane potential difference induced by valinomycin. The proton translocation was inhibited by DCCD, as measured by the quenching of fluorescence of 9-aminoacridine. Studies show that vanadate inhibits the proton gradient driven by ATP hydrolysis in membrane vesicles of M. phlei by interacting with the proteolipid subunit sector of the F0F1-ATPase complex.
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PMID:Purification and functional properties of the DCCD-reactive proteolipid subunit of the H+-translocating ATPase from Mycobacterium phlei. 622 56

Some isolates of the temperature sensitive mutant tsD1 of complementation group D of vesicular stomatitis virus of New Jersey serotype have a nucleocapsid (N) protein which shows an increased electrophoretic mobility on sodium dodecyl sulfate--polyacrylamide gel electrophoresis (SDS-PAGE) when compared with wild type. Utilizing techniques involving specific chemical cleavage at tryptophan or methionine residues, as well as enzymatic cleavage with carboxypeptidases A and B, we have determined that residues near the carboxyterminus are responsible for the electrophoretic difference of the mutant protein. We have further shown that there are no differences in the tryptic peptides of the mutant compared with the wild type or a non-ts revertant in this region of the protein. We have identified a tryptic peptide located outside the relevant carboxyterminal region which is distinct in mutant and revertant. We conclude that the mutation producing the aberrant electrophoretic mobility of N protein of the tsD1 mutant is a missense point mutation located at least 40 amino acid residues from the carboxyterminus and which interacts with a more proximal carboxyregion so as to influence electrophoretic mobility on SDS-PAGE.
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PMID:Characterization of the electrophoretic mobility mutation in the N protein of the tsD1 mutant of vesicular stomatitis virus New Jersey serotype. 629 85

The protein predicted from the DNA sequence of the FBJ murine osteosarcoma virus (FBJ-MSV) onc gene (v-fos) was expressed in Escherichia coli under the control of the tryptophan operon regulatory region. The 381-amino acid protein was identified by synthesis in minicells isolated from bacteria containing the expression vector plasmid. A 52,000-Da protein was made in these minicells, along with the proteins encoded by the beta-lactamase gene present on the expression vector plasmid. Synthesis of the 52K protein was repressed in trpR+ E. coli minicells in the presence of tryptophan, whereas the protein was synthesized under the same conditions in trpR- (derepressed) minicells. The beta-lactamase proteins, however, were synthesized under both conditions. The synthesis of the viral protein, therefore, was directed by the trp operon promoter. The tryptic peptide map of the 52K bacterial protein labeled with [35S]methionine was compared to that of the 35S-labeled protein immunoprecipitated from FBJ-MSV transformed rat cells using tumor-bearing rat sera. The peptide map of the p55 protein, previously identified as a candidate transforming protein in FBJ-MSV transformed cells, matches exactly that of the bacterial 52K protein. The eukaryotic cell protein, however, differs slightly in electrophoretic mobility in SDS gels, most likely due to post-translational modification which does not occur in bacteria.
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PMID:Expression of FBJ-MSV oncogene (fos) product in bacteria. 631 37

Depositing the thermophilic bacterium PS-3 on semi-solid agar plate containing rich medium, several chemotactic rings were formed as in the cases of Escherichia coli and Salmonella typhimurium, indicating that the bacterium is chemotactic. The cells were attracted to L-amino acids: L-alanine, tryptophan, L-aspartate, and glutamate; and to sugars: D-glucose, maltose, D-fructose, and sucrose. In order to find out some sort of methylatable proteins were present, which has been proven to be important in the case of Escherichia coli, the PS-3 cells were labeled with radioactive methionine under conditions in which the protein synthesis had been inhibited. The results showed that the cells contained methylatable proteins of 60,000 to 88,000 daltons. The banding pattern of these methylated proteins was very similar to that of Escherichia coli when the proteins were analyzed by SDS-polyacrylamide gel electrophoresis. In addition, the methyl groups attached onto the proteins were alkaline labile, indicating that the site of methylation was on carboxyl group. The methylation and demethylation reactions of these proteins were affected by the presence of attractants.
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PMID:Chemotaxis in thermophilic bacterium PS-3. 638 29

Glucosylated human serum albumin (G-HSA) obtained under incubation with glucose at 37 degrees C for 8 days showed a new fluorescence with a maximum at 430 nm, resulting in quenching of the fluorescence of only one tryptophan residue on HSA. The quantum yield of new fluorescence is 0.024 at 25 degrees C. The analysis of the excitation spectra allowed us to conclude the absence of energy transfer. In G-HSA, non-disulfide cross-linking hexamer was confirmed by SDS-PAGE.
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PMID:New fluorescence of nonenzymatically glucosylated human serum albumin. 648 18

In the microsome of scallop adductor striated muscle, 30K, 55K, 90K, and 360K proteins were detected as calcium binding proteins by 45Ca autoradiography on the transferred nitrocellulose membrane after sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS PAGE). The 360K protein was directly extracted with Triton X-100 from the whole homogenate of striated portion of scallop adductor muscle and purified through DEAE cellulose and hydroxyapatite column chromatography. This purified scallop high molecular weight calcium binding protein (SHCBP) showed a faster mobility in SDS PAGE in the presence of Ca2+ than in its absence. The decrease of tryptophan fluorescence had a half maximum near pCa 7 and was slightly co-operative with Mg2+. UV absorbance was slightly increased with Ca2+. The CD spectrum also changed with Mg2+ and Ca2+. These results reflect that this SHCBP binds calcium ions under near physiological conditions. SHCBP-like high molecular weight calcium binding proteins were also detected in the smooth muscle portion of adductor muscle and branchiae of scallop by 45Ca autoradiography, but not in liver. The adductor muscle of clam had a high molecular weight calcium binding protein whose molecular weight was a little smaller than that of SHCBP. The foot of turban shell had the same molecular weight calcium binding protein as SHCBP. Stains-all, a cationic carbocyanine dye, which has been reported to stain calcium binding proteins blue, stained SHCBP blue. The spectrum of SHCBP stained with Stains-all was very similar to that of calsequestrin. Although the function of SHCBP is still unknown, it might be expected to correspond to calsequestrin of vertebrate skeletal muscle, a calcium sequestering protein, in the sarcoplasmic reticulum.
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PMID:High molecular weight calcium binding protein in the microsome of scallop striated muscle. 650 Dec 67

Natural and synthetic antioxidants have been shown to repair tryptophan radicals produced from the one-electron oxidation of the free tryptophan amino acid. It has also been observed that both tryptophan and tyrosine radicals in lysozyme can be repaired by these antioxidants to varying degrees of efficiency. Although SDS-solubilized alpha-tocopherol efficiently repairs free tryptophan radicals, it is very inefficient in repairing the amino acids in lysozyme. The rigidity and immobility of solubilized alpha-tocopherol can explain this lack of efficiency.
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PMID:The repair of oxidized amino acids by antioxidants. 650 64


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