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

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

Radiolysis of bovine serum albumin under aerobic and anaerobic conditions was studied by SDS-polyacrylamide gel electrophoresis. After Coomassie Blue or Fast Green staining quantitative evaluations give information about the degradation processes of the protein. Under nitrogen the main reaction is the aggregation caused by covalent cross-links, which includes only a small portion of intermolecular S-S bridges. Under air the radiolysis leads to peptide chain scission, which is not a random process, but yields specific protein fragments. A mechanism for this fragmentation reaction is suggested. The radiation-induced broadening of the serum albumin peak is interpreted as being a result of intramolecular disulfide exchange. In contrast to lactate dehydrogenase the degradation of serum albumin is enhanced by oxygen, probably because of its low tryptophan content.
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PMID:Oxygen effect in the radiolysis of proteins. Part 2. Bovine serum albumin. 660 41

Serotonin-binding protein (SBP) is a soluble protein found in synaptic vesicles of central and peripheral serotonergic neurons. Experiments were undertaken to determine whether serotonin (5-HT) is physiologically stored as a complex with SBP in vivo. [3H]5-HT was used as a probe. Neurons were allowed to specifically take up the labeled amine and attempts were made to recover the in vivo formed [3H]5-HT X SBP complex. Rats were perfused intraventricularly (3 hr) with [3H]5-HT. Strips of rabbit enteric nervous system (ENS) were incubated with [3H]5-HT in the presence of desipramine. The tissues were then homogenized so as to disrupt synaptic vesicles; protein-bound [3H]5-HT was obtained from the 100,000 X g supernatant by filtration on Sephadex G-50 and subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Studies with [3H]5-HT added just prior to homogenization indicated that the [3H]5-HT X SBP complex had formed intraneuronally, prior to homogenization. The protein X [3H]5-HT complexes from brain and gut migrated on the gels with apparent molecular weights of 45,000 and 56,000, corresponding to those measured by SDS-PAGE for purified SBP; however, the 45-kilodalton (kd) molecule predominated when the SBP complex was formed in vivo, whereas the 56-kd molecule predominated when the SBP X [3H]5-HT complex was formed with extracted SBP. It is possible that the 56-kd SBP is characteristic of the molecule in perikarya or nonterminal axons, whereas the 45-kd molecule is characteristic of terminal varicosities because radioautographic results show that in both the central nervous system and ENS, [3H]5-HT is mostly concentrated in terminals. In any case, newly taken up [3H]5-HT preferentially labels 45-kd SBP. Depletion of endogenous 5-HT by placing animals on a tryptophan-deficient diet increased the amount of exogenous [3H]5-HT bound to SBP in vivo. This suggests that endogenous 5-HT is normally bound to SBP and competes with the [3H]5-HT probe for available binding sites. The binding of 5-HT to SBP within vesicles may be important to reduce the osmotic pressure that would build up in synaptic vesicles if 5-HT were free in solution.
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PMID:Storage of serotonin in vivo as a complex with serotonin-binding protein in central and peripheral serotonergic neurons. 661 16

In vitro experiments were performed in order to understand the biochemistry of tryptophan-deficient cataract. Eleven-day-old embryonic chick lenses were cultured in vitro for 3 hr, one and three days in a tryptophan-deficient medium. DNA breakage was followed on sucrose gradient and water-soluble protein synthesis was analysed by SDS-PAGE coupled with fluorography. A medium lacking tryptophan delays the DNA degradation and decreases the synthesis of all soluble proteins including the crystallins.
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PMID:Changes in the DNA breakage and crystallin synthesis of embryonic chicken lenses cultured in a tryptophan-deficient medium. 670 42


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