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)

A factor reacting with SRBC and rabbit IgG was obtained under mild conditions from rat thymus and spleen. The isolation procedure includes incubation of thymocytes or splenocytes with IgG-cellulose adsorbent, destruction of cells, washing the adsorbent and elution of an adsorbed material at pH 2. This preparation as well as the purified substance previously obtained by affinity chromatography on IgG-cellulose columns were found to agglutinate both SRBC and autologous erythrocytes. Preincubation in 1% SDS leads to dissociation of the preparation into several components separated by gel electrophoresis. A probable relation of this structure to the rosette forming capacity of T-lymphocytes is discussed.
Mol Biol Rep 1977 Mar
PMID:The substance reacting with SRBC (sheep red blood cells) and rabbit IgG. Isolation under mild conditions from rat thymus. 85 1

Heterogeneous nuclear ribonucleoprotein particles (HnRNP) were separated in metrizamide density gradients, into two fractions migrating to 1.31 g ml-1 and 1.18 g ml-1, respectively. Proteins associated with each of these fractions were analysed by SDS-acrylamide gel electrophoresis. It is shown that the whole proteins extracted from these two metrizamide fractions exhibit clearly different electrophoretic patterns: 1.31 HnRNP particles contain as major polypeptide chains molecules with molecular weights ranging from 40,000 to 65,000, while major polypeptides of 1.18 HnRNP are banding in the 30,000-40,000 molecular weight region of the gels. Both fractions contain numerous other associated polypeptide chains whose molecular weights are above 65,000. A possible kinetic relationship between these two HnRNP classes was investigated in vivo by performing chase experiments. No clear evidence for a precursor-product relationship was found. Implications arising from these structural and kinetic observations, and problems relating to nuclear maturation of pre-messenger RNA, are discussed.
Mol Biol Rep 1977 Mar
PMID:A comparative study on the two classes of heterogeneous nuclear ribonucleoprotein particles separated in metrizamide density gradient, by electrophoresis of proteins and chase experiments. Evidence for two distinct subfractions of HnRNP in mammalian nuclei. 87 Aug 20

The isolation of rough and smooth endoplasmic reticulum from rat parotid salivary gland is described. The rough membrane was stripped of its bound ribosomes using the KCl-puromycin method. Rough endoplasmic reticulum was reconstituted from stripped-rough membrane and polyribosomes. The reconstituted rough membrane resembled the native rough membrane in the following aspects: RNA/protein ratio, buoyant density in a continuous sucrose gradient and amino acid incorporation capacity. The in vitro synthesis of alpha-amylase by both rough and in vitro reconstituted rough membrane was demonstrated using SDS polyacrylamide gel electrophoresis. The reconstituted rough membrane could be restripped by KCl-puromycin. The in vitro synthesized alpha-amylase remained associated with the rough or the in vitro reconstituted rough membrane, even after these membranes were stripped of their bound ribosomes.
Mol Biol Rep 1976 Jul
PMID:The synthesis of alpha-amylase by rough and in vitro reconstituted rough endoplasmic reticulum derived from rat parotid gland. 95 15

The sedimentation characteristics of polysomal mRNA labelled in vitro by [5-3H]uridine and electrophoretic mobility of similar non-labelled mRNA of mouse plasmacytoma were studied. Rapidly labelled polysomal mRNA may be considered as mRNA on the basis of several independent but indirect tests. These mRNA's are localized in 18-6S region of sucrose gradient. Some part of radioactivity have been found in the ribosomal RNA. It was shown that there is 8-10 RNA fractions in sucrose gradient. The 16S and 12-14S fractions are isolated and partially purified by two- and three-fold centrifugation. Fractions homogenous in sucrose gradient were electrophoresed in PAAG-SDS and divided into several subfractions some of them being common for 16S and 12-14S. The number of non-crossover subfractions was about 2-3. Not less than 20 different main fractions of polysomal mRNA were determined in plasmacytoma cells on the basis of electrophoretic data.
Mol Biol (Mosk)
PMID:[mRNA fractions of mouse plasmacytoma cells]. 95 20

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

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

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


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