Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UNIPROT:P06889 (
Mol
)
630,302
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
After contact with human serum, a series of proteins become exposed on the surface membranes of schistosomula of Schistosoma mansoni as revealed by radioiodination of the intact parasites. Among the proteins, a doublet (Mr 45 000) is particularly prominent. These doublet proteins, which are believed to be parasite-derived, become apparent after a very short time of incubation with human serum (10 min or less) and are expressed on the surface membranes after contact with a high molecular weight component of human serum (Mr greater than 80 000). Pretreatment of the parasites with 1.25 mM colchicine or fixation with 2% glutaraldehyde does not prevent the serum-induced expression of the doublet proteins. Extraction of the parasites with
chloroform
:methanol 2:1 (v/v), however, blocks the human serum effect. Affinity chromatography using immobilized low density lipoproteins (LDL) from human serum shows a tight binding between the 125I-labelled 45 kDa doublet to the LDL. The possible role of the 45 kDa doublet as a receptor for LDL is discussed.
Mol
Biochem Parasitol 1985 Jan
PMID:The interaction of human serum with the surface membrane of schistosomula of Schistosoma mansoni. 398 52
Fatty acid composition of human heart phospholipids was determined in 53 specimens of left ventricular myocardium collected during mitral valve replacement. Ages of the subjects (29 males and 24 females) ranged from 14 to 75 years (mean age = 54). Samples were immediately placed in
chloroform
-methanol 2/1, v/v to which antioxidant was added. Extracted phospholipids were converted to methyl esters which were analyzed by gas liquid chromatography on glass capillary columns. Morphological examination was also performed on 35 out of 53 samples. Age of the patients as well as the morphological state of the organ had no significant effect on major fatty acids in heart phospholipids. No difference by sex was detected. Trans-octadecenoic isomers were detected in all samples but they remained at a low level (0.4% to 1.2% of the total fatty acids).
J
Mol
Cell Cardiol 1985 Aug
PMID:Fatty acid composition of human heart phospholipids: data from 53 biopsy specimens. 404 43
The values reported in the literature for the extramitochondrial ATP/ADP ratio in resting rat-liver mitochondria (State 4) vary widely. The conditions required for an accurate determination of this parameter were therefore investigated. In experiments with rat-liver mitochondria incubated under State-4 conditions, it was found that the extramitochondrial ATP/ADP ratio, as calculated from the values measured in neutralised perchloric acid extracts, was lower than that estimated from the concentrations of creatine and creatine phosphate, using the metabolite indicator method. The discrepancy is due to hydrolysis of ATP occurring in the presence of perchloric acid. Conditions are described for minimising ATP hydrolysis in the presence of perchloric acid, and include the use of low concentrations of perchloric acid, short times of exposure to the acid before neutralisation, low temperatures and the presence of excess EDTA. Under these conditions, the values obtained for the extramitochondrial ATP/ADP ratio agreed with those calculated by the metabolite indicator method, provided ratios do not exceed the value of 100. In cases where the extramitochondrial ATP/ADP does exceed 100, phenol/
chloroform
/isoamyl alcohol must be used to quench the reactions, as described by Slater et al. (Slater, E.C., Rosing, J. and
Mol
, A. (1973) Biochim. Biophys. Acta 292, 534-553). With this method, the extramitochondrial ATP/ADP ratio was found to have a value of more than 1000 in rat-liver mitochondria incubated with succinate + rotenone in the resting state (pH 7.0; T = 37 degrees C), in agreement with Slater et al.
...
PMID:A re-evaluation of conditions required for an accurate estimation of the extramitochondrial ATP/ADP ratio in isolated rat-liver mitochondria. 609 49
The poly (A)-mRNA fraction isolated by
chloroform
deproteinization of liver polysomes and poly(U)-Sepharose chromatography contains a low molecular weights (congruent to 1000) peptidic fraction. The peptides which we suggested to call deprimerones (1) were extracted with 80% ethanol at pH 9.5; after ethanol evaporation, they were purified on Sephadex G-25 column as a fraction of mol. wt. between 1600 and 600, yielding about 9 mg/mg mRNA. If deproteinization is performed with phenol-
chloroform
the yield is about 2 mg/mg mRNA. In Novikoff hepatoma the yield of the same preparation is only 2.7 mg/mg mRNA (about 70% decrease). The obtained deprimerones are active in inhibiting transcription of thymus DNA with E. coli RNA polymerase and [3H]-GTP by about 90% at a ratio peptide/DNA = 2. For comparison the deprimerones obtained previously (2) by extraction of deproteinized DNA inhibit transcription only by about 50% at the same peptide/DNA ratio. The results demonstrated a decrease of the poly (A)-mRNA deprimerone level during carcinogenesis and further support the previously demonstrated specific occurrence of deprimerones with poly(A)-mRNA. They remain in accordance with and provide further support for the deprimerone theory of carcinogenesis postulated earlier (1).
Mol
Biol Rep 1980 Jul 31
PMID:Poly(A)-mRNA deprimerones in rat liver and Novikoff hepatoma cells. 610 57
The mitochondrial Mg2+-activated adenosine triphosphatase (ATPase; EC 3.6.1.4) from the insect flagellate Crithidia fasciculata ATCC 11745 has been extracted from the membrane by
chloroform
treatment and purified to electrophoretic homogeneity by a method involving ammonium sulphate fractionation, gel filtration on Sephadex G-200 and DEAE-cellulose chromatography. The molecular weight of the native enzyme, determined by gel filtration, was about 350 000. Five subunits were detected by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate, with molecular weights of 54 000, 45 000, 35 000, 20 000 and 10 000. The membrane-bound, but not the soluble (F1) ATPase was inhibited by oligomycin and leucinostatin. Both forms of the enzyme were strongly inhibited by the antibiotic efrapeptin and the trypanocidal drug suramin. The inhibition by efrapeptin was of the mixed type, with double-reciprocal plots intersecting below the abscissa, as in the case of the enzyme present in beef heart submitochondrial particles. Suramin, on the other hand, acted as a non-competitive inhibitor of the membrane-bound ATPase and as a strictly competitive inhibitor of the purified F1 ATPase.
Mol
Biochem Parasitol 1981 Oct
PMID:Mg2+-activated adenosine triphosphatase from Crithidia fasciculata: purification and inhibition by suramin and efrapeptin. 611 95
The lysis gene region of bacteriophage lambda, including genes S, R, and Rz, was cloned into the plasmid pBH20. In the recombinant plasmid, the lysis genes are expressed under the control of the lacOP region. Induction of this "lysis operon" with the lac inducer, IPTG, under conditions where transcription from the lacOP region is not subject to catabolite repression, results in a sharply defined lysis after 35 min. Premature lysis can be accomplished by cyanide, chloramphenicol, or
chloroform
, exactly as in bacteriophage lambda infected cells. The lysis gene region of an S- mutant was also cloned into pBH20. Induction of the S- lysis operon has no apparent effect on culture growth; however, large quantities of bacteriolytic activity accumulate intracellularly. Neither cyanide nor chloramphenicol causes lysis in the induced S- clones. Thus premature lysis appears to be entirely an S-dependent phenomenon. A model for the control of lysis in bacteriophage lambda infections is presented in which it is the accumulation of the S gene product in competition with a host "anti-S" protein that determines lysis timing.
Mol
Gen Genet 1981
PMID:Cell lysis by induction of cloned lambda lysis genes. 645 37
The effect of several halomethanes on protein synthesis has been studied in isolated hepatocytes. When cells are added to medium preequilibrated with CCl4 or CBrCl3, protein synthesis is inhibited after a lag period of 4 to 10 min. The concentrations of CBrCl3, CCl4, and
CHCl3
which cause a 50% inhibition of protein synthesis are about 6 microM, 400 microM, and 4 mM, respectively. This order of potency parallels the rate at which these compounds are metabolized by the hepatic mixed function oxidase, suggesting that metabolism is required for toxicity. The inhibitory effect caused by 18 min of exposure to CBrCl3 is not reversed when the toxin is removed, indicating that inhibition involves some irreversible modification of cellular material. Unexpectedly, the inhibitory effect caused by 18 min of exposure of CCl4 is about 30-40% reversed when the toxin is removed. This suggests that CCl4 causes inhibition not only by a metabolism-dependent (irreversible) pathway, but by a metabolism-independent (reversible) mechanism as well. Extracellular Ca2+ is not required for CCl4 inhibition of protein synthesis.
Exp
Mol
Pathol 1984 Dec
PMID:Halomethane-induced inhibition of protein synthesis in isolated hepatocytes. 651 May 7
Polysaccharides and other complex carbohydrates were released by proteolysis of the
chloroform
-methanol insoluble residue of 10 day-old worms and eggs of Hymenolepis diminuta. Gas-liquid chromatographic analysis of alditol acetate derivatives of monosaccharides released from the polysaccharides by hydrolysis revealed that in the 10 day-old worm, glucose was the most abundant sugar, followed by galactose, glucosamine, galactosamine, fucose and possibly rhamnose. Mannose was least abundant and xylose was absent. In the egg, glucose and galactose were equally abundant, followed by the same sugars found in 10 day-old worms, and xylose was present. Uronic acid was detected in both fractions by specific chemical tests. None of the saccharide material from eggs and worms was susceptible to degradation by Streptomyces hyaluronidase, chondroitinase AC, and slightly susceptible to chondroitinase ABC, as shown by electrophoretic analysis on composite 2.2% acrylamide-agarose slab gels and 4.5/12.5% polyacrylamide gels before and after enzymatic treatment. One of the gel-separable bands, however, was degradable by both nitrous acid and Flavobacterium heparinase. Both bands from eggs were degradable by nitrous acid. These results suggest that eggs contain heparin and/or heparan sulfate and perhaps dermatan sulfate and that 10 day-old worms also have these polyglycans but possibly not chondroitin sulfate or hyaluronic acid.
Mol
Biochem Parasitol 1984 Jan
PMID:Characterization of polysaccharides of the eggs and adults of Hymenolepis diminuta. 653 86
DNA isolated from rat liver by intensive deproteinization with
chloroform
/isoamyl alcohol and phenol contains low molecular weight peptides in a quantity of about 20 micrograms/mg DNA. These peptides show high specific activity in inhibiting transcription in a reconstituted cell-free system with prokaryotic and eukaryotic RNA polymerase. Their level is markedly decreased in DNA prepared from Novikoff hepatoma cells. Moreover the amino acid analysis and the pattern of analytical separation by high performance liquid chromatography (HPLC) show some biochemical differences between DNA-binding peptides extracted from rat liver and Novikoff hepatoma cells. The possibility that carcinogenesis may involve mechanisms which lead to selective removal of some components of the DNA-binding peptides, is discussed.
Mol
Biol Rep 1983 Aug
PMID:DNA-binding peptides from rat liver and Novikoff hepatoma cells: quantitative level and possible biochemical differences. 668 24
Adult Schistosoma mansoni were shown to synthesize a peptide containing lipid against which an antiserum could be raised in rabbits. The proteolipid purified by silicic acid chromatography was soluble in
chloroform
/methanol mixtures, it was very hydrophobic and contained fatty acids in its molecule, as well as other unidentified neutral lipids.
Mol
Biochem Parasitol 1983 Mar
PMID:The occurrence of proteolipid antigens in Schistosoma mansoni. 688 25
<< Previous
1
2
3
4
5
6
7
8
9
10
Next >>