Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Analysis of proteins in nucleoli and chromatin of mouse ascites tumor cells labeled with [32P]orthophosphate by SDS-polyacrylamide gel electrophoresis showed that a highly radioactive protein was localized in the nucleoli. This protein was purified and the final preparation appeared as a single component on hydroxylapatite column chromatography with or without SDS. This protein was found to be a nucleolus-specific phosphoprotein with a molecular weight of 120 000. The phosphate moiety in this protein turned over very rapidly whereas the protein itself was stable. When the nucleoli were disrupted by EDTA treatment, this unique protein was found as a major protein constituent of the ultracentrifugal supernatant.
Mol Biol Rep 1976 Nov
PMID:A nucleolus-specific phosphoprotein in mouse ascites tumor cells. 101 75

Transient short-lived species arising in chlorophyll-protein complexes of PS I on flash excitation were studied by means of flash-photolysis and luminescence methods. Complexes were isolated from chloroplasts by the solubilisation in SDS and subsequent electrophoresis. Three different types of reactions associated with: a) the triplet state of monomeric chlorophyll; b) redox reactions in reaction centres; c) photochemical reactions of monomeric chlorophyll were established on excitation. The arrangement of different forms of chlorophyll connected with the protein globule is discussed.
Mol Biol (Mosk)
PMID:[Transient states in the photoreactions of chlorophyll-protein complexes]. 105 65

A mutation affecting the activity of the first enzyme in glutathione biosynthesis in E. coli K 12 has been mapped. The mutant allele called gshA is located by transduction in the pheA-nalB segment. The linkages with pheA and tyrA provide a convenient method for transfer of gshA to other strains and so introduce a very low level of non-protein sulfhydryl groups into the E. coli cells.
Mol Gen Genet 1975 Nov 24
PMID:Mapping of gshA, a gene for the biosynthesis of glutathione in Eschericha coli K12. 110 13

Nuclear 14 S RNP particles containing poly (A) from Ehrlich ascites carcinoma cells and rat liver were purified by re-sedimentation in sucrose gradients, by Cs2SO4 density gradient centrifugation and by affinity chromatography on a poly (dT)-Sepharose column. Proteins of these RNP particles were electrophoresed in urea and SDS-polyacrylamide gels. RNP particles of ascites carcinoma cells contain two main bands having molecular weights of 51 000 and 69 000 daltons, respectively, and two or three minor components.
Mol Biol Rep 1975 Mar
PMID:Protein composition of nuclear 14 S ribonucleoprotein particles containing poly (A). 112 12

Total polysomal RNA or poly(A)-containing RNA isolated from membrane-bound polysomes of normal lactating rabbits directed the synthesis of casein in a reticulocyte lysate. Casein was identified by immunoprecipitation followed by SDS-polyacrylamide gel electrophoresis of the immunoprecipitate. The poly(A)-containing RNA was heterogeneous with one major peak corresponding to a 12-S sedimentation coefficient as determined by polyacrylamide gel electrophoresis. Using the same procedure, mRNAs isolated from the non-secreting tissue of pseudopregnant rabbits were found not to contain the 12-S peak and were unable to direct the synthesis of casein in vitro. Prolactin injected into pseudopregnant rabbits induced the synthesis of proteins immunoprecipitable by anti-casein anti-serum and induced the simultaneous appearance of the 12-S mRNA. Progesterone injected with prolactin prevented the induction of casein synthesis and the appearance of mRNA for casein. A close relationship was established between the ability of the tissue to synthesize immunoprecipitable casein and the corresponding mRNA content of polysomes.
Mol Cell Endocrinol 1975 Jul
PMID:Regulation of casein synthesis in the rabbit mammary gland. Titration of mRNA activity for casein under prolactin and progesterone treatments. 114 19

Oocytes from Xenopus laevis were injected with polysomes from normal human term placenta. Synthesis of the protein hormone Human Placental Lactogen (HPL) in the oocytes was demonstrated by specific immunoprecipitation with anti-HPL serum. Analysis of the immunoprecipitates on SDS-polyacrylamide gel revealed one peak, with a migration distance corresponding exactly to that of [14C]-Radioacetylated HPL added as a marker. Two days after injection the mRNA was still able to direct the synthesis of HPL.
Mol Biol Rep 1976 Apr
PMID:Synthesis of human placental lactogen in Xenopus oocytes. 127 64

Western blot analysis showed that the monoclonal antibody 2D7.10 recognized lipophosphoglycan (LPG) from Entamoeba histolytica HM-1:IMSS. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) pattern of [3H]galactose-labeled LPG and Western blot analysis of total lysate of E. histolytica with 2D7.10 revealed patterns similar to that of LPG with 2D7.10. This antibody could also immunoprecipitate purified LPG from the strain HM-1:IMSS after biosynthetically labeling with [3H]galactose and [32P]orthophosphate. However, no immunoprecipitation was observed when 2D7.10 was incubated with [32P]orthophosphate-labeled purified LPG from strain 200:NIH. Sera from patients suffering from invasive amoebiasis also immunoprecipitated 32P-labeled, purified LPG and could immunostain this molecule in Western blots. The human immune sera recognized carbohydrate epitopes but not the associated polypeptides of LPG, as evidenced by sensitivity to periodate digestion, mild acid hydrolysis but not to pronase treatment. It was earlier shown that 2D7.10 binds a carbohydrate epitope in a subset of axenized pathogenic strains of E. histolytica and that this epitope undergoes changes when cultured along with bacteria. These observations suggest that the E. histolytica LPG contains a strain-specific, variable epitope and that LPG is immunogenic in human.
Mol Biochem Parasitol 1992 Dec
PMID:Recognition of Entamoeba histolytica lipophosphoglycan by a strain-specific monoclonal antibody and human immune sera. 128 4

The level of two thioesterases, acyl-CoA thioesterase and acyl-ACP thioesterase was determined during seed maturation in oil seed rape. Both thioesterase activities rose markedly prior to the onset of lipid accumulation, but the induction kinetics suggest that the activities reside on distinct polypeptides. Acyl-ACP thioesterase (EC 3.1.2.14) was purified 2000-fold using a combination of ion exchange, ACP-affinity chromatography, chromatofocusing and gel filtration. Using native gel electrophoresis, and assays for enzymic activity, two polypeptides were identified on SDS-PAGE as associated with the activity. Cleveland mapping of these polypeptides, of 38 kDa component and 33 kDa respectively, demonstrated that they are related. An antibody was prepared against the 38 kDa component, and this also recognises the 33 kDa polypeptide in highly purified preparations. Western blotting of a crude extract identifies one band at 38 kDa consistent with the 33 kDa component being a degradation product generated during purification. The native molecule has a M(r) of 70 kDa indicating a dimeric structure. The enzyme has a pH optimum of 9.5 and shows strong preference for oleoyl-ACP as substrate. The intact enzyme has an N-terminus blocked to protein sequencing. We also found that two other polypeptides co-purify with acyl-ACP thioesterase under native conditions. The N-terminal amino-acid sequence of these polypeptides is shown and their possible identity is discussed.
Plant Mol Biol 1992 Dec
PMID:Induction, purification and characterisation of acyl-ACP thioesterase from developing seeds of oil seed rape (Brassica napus). 130 Oct 73

Previous studies have shown degradation of cardiac structural proteins and disruption of the sarcolemma as a result of acute myocardial infarction. However, there is no evidence to date on changes in sarcolemmal membrane proteins induced by experimental subacute myocardial infarction. We studied subepicardial layers overlying myocardial infarct 4 days following ligation of the left anterior descending coronary artery in 12 dog hearts. We first demonstrated that this layer provides the anatomic-electrophysiologic substrate for reentrant arrhythmias using activation mapping techniques and histologic correlations. The makeup of membrane proteins was studied using SDS polyacrylamide gel electrophoresis, peptide mapping, and laser densitometry. Sarcolemmal membrane proteins were isolated by ultracentrifugation through a sucrose gradient. We found that a sarcolemmal polypeptide (MW 126,000; n = 12) in the normal tissues has a different mobility than the corresponding protein (MW 124,000; n = 12) of the ischemic tissues although their peptide analysis appeared similar, suggesting that the protein undergoes a post-translational modification. In addition, two proteins (MW 75,000; n = 12 and MW 88,000; n = 12) were present in greater amount in the ischemic than in the control tissues suggesting either acceleration in protein synthesis or slow down of degradation turnover. These results demonstrate that specific changes occur in membrane proteins subjected to ischemic insults which might be responsible for membrane alterations following ischemia and may contribute to the abnormal electrophysiologic properties and arrhythmia seen in vivo at this stage.
Cell Mol Biol 1992 Sep
PMID:Changes in sarcolemmal proteins in subacute myocardial infarction in the dog. 130 6

We have purified a topoisomerase activity from broccoli (Brassica oleracea var. italica) to near homogeneity. The enzyme is an 80 kDa monomer as judged by gel filtration chromatography and SDS gel electrophoresis, though it may represent a proteolytic fragment of a larger protein. The enzyme is capable of removing both negative and positive supercoils in steps of one, does not absolutely require Mg2+, is only very weakly stimulated by NaCl, is inhibited by camptothecin, and cross-reacts with an antibody directed against human DNA topoisomerase I. These properties identify the enzyme as a eukaryotic type I topoisomerase.
Plant Mol Biol 1992 Mar
PMID:Purification and properties of DNA topoisomerase I from broccoli. 131 91


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