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)

The final step in the biosynthesis of phosphatidylethanolamine, the major membrane lipid of Escherichia coli, is catalyzed by the membrane-bound enzyme, phosphatidylserine decarboxylase. A variation of a procedure for localized mutagenesis (Hong and Ames, 1971) was employed to generate conditional lethal mutants in phosphatidylserine decarboxylase. In our modification, an episome carrying the psd gene closely linked to purA+ was heavily mutagenized in vivo in a strain also lysogenic for phage P1CMclr100. After induction of a phage lytic cycle, the purA+ marker was transduced to a purA- recipient. A majority of the Pur+ transductants thus contained a psd gene originating from the heavily mutagenized episomal strain. Three mutants were isolated in which temperature-sensitive growth is caused by thermosensitive phosphatidylserine decarboxylase activity that is defective in vivo at the non-permissive temperature. All 3 mutations were mapped at the same location as psd1, being cotransduced with melA, purA, and ampA. The gene order in this region, as determined by a phage Pl-meidated, three-factor cross is ampA-psd-purA. psd+ is dominant to the psd mutant alleles.
Mol Gen Genet 1976 Nov 17
PMID:Conditional lethal phosphatidylserine decarboxylase mutants of Escherichia coli. Mapping of the structural gene for phosphatidylserine decarboxylase. 79 63

The prostate glands of rats, mice, guinea pigs and hamsters were found to be a rich source of enzymes catalyzing the Mn2+-dependent transfer of galactose from UDP-galactose to glycoprotein acceptors such as ovomucoid and ovalbumin. The ventral prostate was also very active in promoting transfer of fucose from GDP-fucose to ovomucoid. The prostatic enzymes promoting both galactosyl and fucosyl transfers to glycoproteins were very largely membrane-bound, and were markedly activated by the non-ionic detergent Triton X-100. Castration of adult male resulted in a many-fold and roughly parallel decline in both glycosyltransferase activities over a period of two weeks, which was reversed by subsequent daily treatment with testosterone for 8 days. The very low galactosyltransferase of the ventral prostate of hypophysectomized rats was markedly enhanced by testosterone administration, whereas prolactin alone or in combination with androgen had no significant effect.
Mol Cell Endocrinol
PMID:Glycoprotein glycosyltransferases in male reproductive organs and their hormonal regulation. 82 97

Ribosomal proteins from pure free and membrane-bound rat liver polysomes were analyzed with a highly resolutive two-dimensional gel electrophoresis technique, using sodium dodecyl sulfate in the second dimension. Three acidic proteins found in free polysomes were always absent from the membrane-bound polysomes. Their molecular weights were estimated to be 20 000, 19 500 and 18 500. When free ribosomes were dissociated into subunits, the three protein spots were still found in the 60S subunit pattern, but they were weaker than in polysomes. A possible involvement of these three proteins in the attachment of ribosomal structures to the membranes is proposed.
Mol Biol Rep 1977 Jun
PMID:Comparison of the protein content of free and membrane-bound rat liver polysomes and of the derived subunits. 88 99

Chloroplasts from spinach can be separated into at least three different populations by countercurrent distribution using polymer two-phase systems. The chloroplast particles of the three populations differ in protein/chlorophyll ratio, ultrastructure and metabolism. One population, peak I, consists of intact chloroplasts surrounded by the chloroplast envelope; the second population, peak II, consists of chloroplasts, which have lost their envelopes and much of their stromal material; the third population, peak III, consists of particles containing intact chloroplasts surrounded by a membrane-bound cytoplasmic layer including mitochondria and peroxisomes. Rapid batch procedures of peak I chloroplasts incorporated 14C almost entirely into glycolate and intermediates of the Calvin cycle and starch synthesis. Only small amounts were found in sucrose and amino acids. On the other hand preparations of peak III chloroplasts have a much broader spectrum of 14C-labelled products. Sucrose, malate and some amino acids contained about 40% of the 14C incorporated. It is concluded from these experiments that sucrose is formed not within the chloroplast but in the cytoplasm from intermediates exported by the chloroplast. The origin of peak III particles and their use for studying the cooperation between the chloroplast and the surrounding cytoplasm including mitochondria and peroxisomes is discussed.
Mol Cell Biochem 1976 Jun 15
PMID:Properties of chloroplasts isolated by phase partition. 94 May 50

Proteins present in messenger ribonucleoprotein particles were labeled with [35S]-methionine in Ehrlich ascites tumor cells in which synthesis of new ribosomes was inhibited. Poly(A)-protein complexes were isolated from free and membrane-bound polyribosomes by sucrose gradient centrifugation and affinity chromatography on oligo(dT)-cellulose. Both classes of Poly(A)-protein particles contain a poly(A) chain of about 70 adenyl residues and a protein with a molecular weight of 76000 attached to it.
Mol Biol Rep 1976 Sep
PMID:Characterization of poly(A)-protein complexes isolated from free and membrane-bound polyribosomes of Ehrlich ascites tumor cells. 103 5

UV-light is shown to induce the structural transitions in the erythrocyte membrane described by S-shape curves in plots of the structural response versus the irradiation dose. In contrast to the free acetylcholine esterase (AChE) UV-light acts on the membrane enzyme as a mixed inhibitor (simultaneous change in Vmax and Km). The modification of the environment structure of residual enzyme is suggested to be the main reason of this phenomenon. The effect is under the control of membrane integrity and disappears after its desintegration. Membrane AChE treated ultrasonically both prior to and after irradiation is inactivated without a Km change. The data obtained show the influence of erythrocyte membrane structure on the catalytic behaviour of membrane-bound AChE.
Mol Biol (Mosk)
PMID:[Influence of UV-light on erythrocyte membrane structure and catalytic behaviour of membrane acetylcholine esterase]. 105 67

Rhodopsin biosynthesis and transport in the photoreceptor cell have been analyzed by subcellular fractionation of frog retinas after short periods of radioactive amino acid incorporation in vivo. Labelled membrane proteins were identified by autoradiography or sodium dodecyl sulfate-polyacrylamide gels. One of the most intensly labeled proteins in retina had a molecular weight comparable to opsin isolated from purified rod outer segments (ROS). Incorporation of label into this protein was rapid; the relative specific activity then diminished after the first 2 hr as radioactivity was transferred from retinal subcellular fractions to ROS. The kinetics of this transfer resembled rates previously observed by Hall et al. (Hall, M. O., Bok, D., and Bacharach, A.C.E. (1969), J. Mol. Biol. 45, 397). To identify the rapidly labeled protein as opsin we devised a new technique of two-dimensional immunoelectrophoresis of detergent solubilized membrane proteins. Antibodies were prepared against both whole ROS and opsin. After initial separation of retinal proteins on sodium dodecyl sulfate-polyacrylamide gels, a second dimension of electrophoresis in agarose, containing antisera, resulted in the formation of specific immunoprecipitates. Immunochemical analysis of all membranous and soluble retinal subcellular fractions indicated that newly synthesized opsin was membrane bound upon completion of synthesis. At no period of incorporation was a soluble form of newly synthesized opsin detectable. On this basis, we suggest that this protein is apparently transported as a water-insoluble membrane-bound molecule through the cytoplasm or along membranes of the inner segment to its assembly site near the base of the outer segment.
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PMID:Membrane biosynthesis in the frog retina: opsin transport in the photoreceptor cell. 107 39

Plasma glycoprotein synthesis in the liver occurs in a stepwise fashion. The first sugar, N-acetyl-glucosamine, is attached to the protein during the growth of the polypeptide chain on the membrane-bound ribosomes. Subsequent carbohydrates are incorporated after the completion of the protein in the lumen of the endoplasmic reticulum and Golgi apparatus. The reactions are carried out by enzymes strongly bound to the membranes. Because the glycosylation reaction occurs in the interior of the cytoplasmic tubules a permeability problem for the nucleotide sugar exists. Recent studies indicate that sugar-lipids are formed on the cytoplasmic site of the membrane and these complexes transfer the sugars across the membrane. Experimental evidence for this pathway is presented in this article.
Mol Cell Biochem 1975 Jan 31
PMID:A proposed pathway of plasma glycoprotein synthesis. 112 82

1. Membrane-bound and free polyribosomes were isolated from parathyroid glands of normal dogs by a discontinuous density-gradient technique. 2. The conditions necessary for optimum incorporation by bound and free ribosomes of [3-H]-phenylalanine into protein were determined for assays in vitro directed by both endogenous messenger ribonucleic acid (mRNA) and polyuridylic acid [poly(U)]. 3. When the specific cofactors were available in optimum amounts, the rate of incorporation of amino acids into protein was directly proportional to the number of ribosomes present. This applied to assays directed by endogenous mRNA and poly-(U). 4. The results indicate that it is possible to isolate and directly study the protein synthetic activity of membrane-bound and free parathyroid ribosomes.
Clin Sci Mol Med 1975 May
PMID:Protein synthetic activity of membrane-bound and free ribosomes from parathyroid glands of dogs. 112 29

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


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