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)

1. Human gastrointestinal secretions formed soluble copper complexes when labelled in vitro with 64Cu. 2. Copper-binding substances of low molecular weight were demonstrated in the saliva, gastric juice and secretin-stimulated duodenal aspirate of nomal subjects by dialysis and gel-chromatography studies. 3. The nature of the copper complexes formed by secretions obtained from patients with Wilson's disease was similar to that oc complexes formed by secretions of normal subjects. 4. Bile contained a copper-binding fraction of high molecular weight which was more concentrated in gall-bladder than hepatic bile. Between pH 5 and pH 8, this component had a greater binding affinity EDTA at a concentration of 10 mmol/1. 5. Absorption of 64Cu from 64Cu-labelled saliva, gastric juice or L-histidine solution (100 mmol/1) administered intraduodenally into groups of rats was similar to that observed in a control series given [Cu]cupric acetate in sodium chloride solution. In contrast, the absorption of 64Cu from labelled hepatic and gall-bladder bile was significantly reduced. 6. The results suggest that dietary copper forms soluble complexes with the alimentary secretions and that these complexes influence absorption of the metal according to their molecular size. The net uptake of ingested copper from the gut lumen ms, low-molecular-weight ligands in the alimentary secretions and a macromolecular copper-binding complex of bile.
Clin Sci Mol Med 1975 Sep
PMID:Studies on the nature of complexes formed by copper with human alimentary secretions and their influence on copper absorption in the rat. 24 May 30

The ribosomal proteins of 11 mutants which are sensitive to starvation at elevated temperature and of 36 transductants derived from them were studied with several electrophoretic, immunochemical and proteinchemical methods. The following results were obtained: (1) Ribosomal protein S8 is altered in three of these mutants. (2) The amino acid exchange in proteins S8 of mutant N4128 is Glu leads to Lys in position 59 of the protein chain. (3) Temperature sensitivity and inability to recover from starvation at elevated temperatures are caused by the same mutational event which is, however, unrelated to the alteration in protein S8. Several electrophoretic and immunological procedures were applied during the characterization of these mutants. A modified immunoelectrophoresis on cellulose acetate gels was developed, and proved to be the most applicable procedure for the detection of mutationally altered ribosomal proteins. This procedure may gain general importance for detecting mutational alterations in other proteins.
Mol Gen Genet 1977 Dec 30
PMID:Improved electrophoretic and immunochemical techniques for the identification and characterization of mutant proteins, applied to ribosomal protein S8 in Escherichia coli mutants. 34 Sep 33

The peptide-chain elongation rate of Saccharomyces cerevisiae at two different growth rates was estimated by the kinetics of radioactive labelling of nascent and finished polypeptides as described by Gausing, 1972, and Young and Bremer, 1976. The elongation rates of a diploid strain cultured in yeast nitrogen base supplemented with glucose or acetate were 9.3 amino acids/s and 5.5 amino acids/s at 30 degrees C, respectively. These data together with published values on the "ribosomal efficency" as a function of growth rate (Waldron and Lacroute, (1975) enable us to estimate the rate of synthesis of ribosomal proteins as a function of the rate of total protein synthesis, alpha r, and the fraction of ribosomes that one active in protein synthesis. We conclude that in S. cerevisiae alpha r is largely independent of the growth rate while the fraction of active ribosomes decreases with decreasing growth rate.
Mol Gen Genet 1979 Feb 26
PMID:Peptide chain elongation rate and ribosomal activity in Saccharomyces cerevisiae as a function of the growth rate. 2787 2

Two sB mutations in the genome of bacteriophage fd were located by sequence analysis in the fd sequence at positions 971 and 6341. Base changes at or close to these positions in phage M13 and in phage fl am 124 also correlate with a loss of sensitivity to B restriction. From the sequence homology between the sequences at the two sB sites the recognition signal for the E. coli B restriction/modification enzzyme is predicted to be: 5' TGA---8N---TGCT 3' 3' ACT---8N---ACGA 5'.
Mol Gen Genet 1979 Jan 11
PMID:Nucleotide sequence of the recognition site of the B-specific restriction modification system in E. coli. 37 93

Treatment of unanesthetized castrated adult male rats every 3 h for 48 h with either 5 microgram of arginine vasotocin (AVT) and/or 1 microgram luteinizing hormone-releasing hormone (LRH) caused a significant inhibition of plasma levels of luteinizing hormone (LH) and compared to castrated control rats receiving diluent only. However, the intravenous (iv) injection of 1 microgram of AVT into urethane-anesthetized male rats which had been castrated for 0, 24 or 48 h did not affect plasma levels of LH at 10, 20 or 60 min following injection compared to their respective diluent-treated castrated control rats. Similarly, the iv injection of either 100 ng, 1 microgram or 10 microgram AVT was unable to acutely affect plasma levels of LH in intact male rats. Following the iv injection of 2 doses of 50 ng LRH spaced 1 h apart in anesthetized castrated male rats, 2 peaks of equal magnitude in plasma LH were noted. Castrated rats treated with 2 injections spaced 1 h apart of LRH + AVT had significantly higher plasma levels of LH than did rats treated with LRH alone. In subsequent studies, both AVT and arginine vasopressin were observed to augment the plasma response of LH to an injection of LRH whereas oxytocin had no effect. A single injection of AVT + LRH significantly augmented the plasma titers of LH compared to levels observed in LRH-treated control rats as did a second injection 1 h later. The administration of cyproterone acetate sc for 2 days by itself had no effect on plasma LH but in conjunction with LRH caused a marked rise in plasma LH compared to intact rats treated with LRH alone. AVT in combination with LRH and cyproterone acetate caused a significant elevation in plasma LH at 60 min post-injection when compared to plasma levels of rats treated with LRH alone or the combination of LRH and cyproterone acetate. It is concluded that acute intravenous injections of AVT augment the LH-releasing activity of LRH; chronic treatment for 48 h, however, with LRH + AVT leads to a significant depression of plasma LH perhaps due to an exhaustion of the releasable pool of LH in the anterior pituitary.
Mol Cell Endocrinol 1979 Apr
PMID:Interaction of luteinizing hormone-releasing hormone, cyproterone acetate and arginine vasotocin on plasma levels of luteinizing hormone in intact and castrated adult male rats. 37 36

RNA synthesis, correlation of various histones and acetylation and phosphorylation of the chromatin proteins were studied in the rat heart during monthly hypothyroidism. It was shown that [3H]uridine incorporation into heart RNA decreases considerably at hypothyrosis. The alteration in relative amounts of the histone H4 subfractions, which does not depend on the method of hypothyrosis reproduction (inhibition of thyroid function by 1-methyl-2-mercaptoimidazole, thyroidectomy) was detected by the method of analytical electrophoresis in 15% polyacrylamide gels containing 3.125 M urea and 0.9 N acetic acid. Increased incorporation of [32P]phosphate into histone fraction H2b and total fraction of acidic chromatin proteins was observed in vivo. Increased incorporation of labeled acetate into the total histone fraction and reduced incorporation into acidic nuclear proteins were obtained. It was shown that the increased incorporation of acetate into the total histone fraction was due to the increased acetylation of histones H3, H2b, H4 and acid-soluble chromatin proteins characteristic of tissues with a low level of replication. It is assumed that the observed changes of nuclear proteins reflect the process of chromatin reorganization caused by a prolonged deficiency of thyroid hormones.
Mol Biol (Mosk)
PMID:[RNA synthesis and modifications of heart nuclear proteins during thyroid hormone deficiency]. 46 Jan 95

The distance between fluorescein mercuric acetate (FMA), attached to the HS-group of Fe- and Mo-Fe-protein, and the nearest iron-sulphur cluster (ISC) was determined. For Fe-protein the distance was 18--20 A and for Mo-Fe-protein 12--14 A. The distance between Fe-protein FMA and the nearest Mo-protein ISC determined by complementation of the labelled Fe-protein and native Mo-Fe-protein was 14--16 A. The distance between MO-OFe-protein ISC and complement Fe-protein ISC was 18--20 A. A te-protein ISC permitted to suppose that the electron was transfered from Fe-protein ISC to Mo-Fe-protein ISC by the contact of the ISC or with the help of ATP molecule.
Mol Biol (Mosk)
PMID:[Estimation of the distance between the iron-sulfur cluster of Fe-protein and the nearest iron-sulfur cluster of Mo-Fe-protein of nitrogenase on the basis of the inductive-resonance theory of energy transfer]. 50 57

An androgen receptor has been characterized in the cytosol fraction of testes from hypophysectomized adult rams after in vitro labelling with [3H]testosterone. It can be distinguished from the testicular androgen-binding protein (ABP) and from the plasma 5 alpha-dihydrotestosterone-binding protein by electrophoresis on 3.25% acrylamide gels (Rx = 0.5) and on agar gels (anodic migration). It sediments in the 4S region in sucrose gradient containing 0.4 M KCl. Its complex with testosterone dissociates very slowly (t 1/2 = 29 h at 0 degrees C), and is destroyed by heating at 50 degrees C for 30 min and by pronase. Its relative affinities for steroids are 5 alpha-DHT greater than T greater than 5 alpha-androstanediols greater than cyproterone acetate greater than estradiol greater than progesterone. The number of binding sites is limited (about 20 fmoles/mg protein) and the apparent equilibrium dissociation constant (KD) is 5 x 10(-9) M.
Mol Cell Endocrinol 1979 Nov
PMID:Characterization of a cytoplasmic androgen receptor in the ram testis. 51 Jul 71

Apl, a gene involved in the processing of lysosomal acid phosphatase in mouse liver, has been mapped on Chromosome 17. The gene order and map distances in per cent recombination of the loci studied are T (20.6 +/- 3.4) Pgk-2 (7.4 +/- 2.2) Apl. Thus, Apl is at least 7 cM distal to H-2 on this chromosome. In addition, strain-specific allelic variants for Apl have been demonstrated on cellulose acetate gels, a quick and inexpensive method of electrophoresis.
Mol Gen Genet 1977 Oct 24
PMID:Liver-specific lysosomal acid phosphatase deficiency (Apl) on mouse chromosome 17. 60 Feb 62

Thirteen chromosomal loci have been identified which affect acetate metabolism in Coprinus. Mutants at only two loci, acu-l and acu-7, are deficient in isocitrate lyase (ICL) (EC 4.1.3.1) activity. acu-1 mutants are unable to induce ICL because they lack acetyl-CoA synthetase which is required to convert acetate to the metabolic inducer of ICL. acu-7 is the structural gene for ICL. This was shown by selecting temperature sensitive acu+ revertants resulting from a second mutation within the acu-7 gene. One such revertant was shown to produce an ICL protein which was more thermolabile than the wild type enzyme. Other workers have postulated that ICL activity is important during asexual morphogenesis in fungi. No evidence was found for this in Coprinus. The morphological mutant oidial, which produces abundant asexual spores even in submerged culture, had the same low uninduced level of ICL activity as the wild type. Moreover, an acu-7 mutation had no effect on the expression of the oidial phenotype.
Mol Gen Genet 1977 Dec 09
PMID:Genetics and function of isocitrate lyase in Coprinus. 60 Feb 68


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