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)

Two strains independently isolated in Salmonella typhimurium display abnormal autolytic activity when nutrient broth becomes alkaline. They also show increased sensitivity to deoxycholate, EDTA, and sodium dodecyl sulfate. Response to acridine orange remains normal. In both strains a single stable mutation is responsible for all the changes. The same gene, called envD, appears to be involved in both mutant strains. envD has been located at minute 33 of the Salmonella genetic map, between markers sucA and nadA, very close to the latter. envD also affects morphological characteristics of the cells. Many mutant cells are shorter than wild type bacteria, and appear frequently associated in short chains of 4 to 10 cells. Furthermore, envD mutants display division by septation under conditions that preclude its observation in wild type strains.
Mol Gen Genet 1976 Feb 27
PMID:Envelope mutation promoting autolysis in Salmonella typhimurium. 0 22

Proteins of yeast cytoplasmic ribosomes were analyzed by two different methods of two dimensional gel electrophoresis: run at pH 8.6 in 1-D1 and at pH 4.6 in 2-D (Method A); run at pH 5.0 in 1-D and in the presence of sodium dodecyl sulfate in 2-D (Method B). The numbers of proteins estimated were 28 (Method A) and 29 or 30 (Method B) in the 40S small subunit, and 40 (Method A) and 41 (Method B) in the 60S large subunit, respectively. Molecular weights of proteins in the small and the large subunits were found to be less than 40,000 and 60,000 respectively.
Mol Gen Genet 1976 Apr 23
PMID:Study on proteins from yeast cytoplasmic ribosomes by two-dimensional gel electrophoresis. 0 66

Two distinct steroid-binding proteins are present in rabbit plasma. One of the proteins (TeBG) binds [3-H]5 alpha-dihydrotestosterone (5 alpha DHT) and [3-H]testosterone. The affinity of this binding protein for 5 alpha DHT was 3-4 times greater than for testosterone. Binding of [3-H]5 alphaDHT could be inhibited by unlabeled 5 alpha DHT, testosterone, 5 alpha-androstan-3 alpha,17 beta-diol (3 alpha-diol), and 17 alpha-methyl- B-testosterone (skf) 7690). The relative affinity of the competitors was: 5 alpha DHT greater than 3 alpha-diol greater than testosterone greater than SKF 7690. The antiandrogens, cyproterone (1,2 alpha-methylene-6-chloro-pregn-4,6-diene-17 alpla-ol-3,20 dione), cyproterone-17-acetate, and 6 alpha-bromo-17 beta-hydroxy-17 alpha-methyl-4-oxa-5 alpha-androstan-3-ine (BOMT) were ineffective in competing for [3-H5d alpha DHT binding sites, as were 4-androstene-3, 17-dione, 17 beta-estradiol (E2), progesterone, and cortisol. The formation of the [3-H]5 alpha DHT-TeBG complex was extremely rapid; the binding reaction was essentially completed in 15 s. The complex dissociated rapidly in the presence of charcoal. The dissociation rate constant (Kdiss) was 0.157 min- minus 1 and the dissociation half-time t-1/2) was 4.5 min. In the presence of charcoal and unlabeled 5 alpha DHT the Kdiss was 0.268 min- minus 1 and the t=1/2 was 2.6 min. The sedimentation coefficient of TeBG was congruent to 4.6 S and its molecular weight, estimated by gel filtration on a calibrated Sephadex G-200 column, was congruent to 75,000. The concentration of TeBG in male rabbit plasma decreased with sexual maturation and was approximately three times higher in adult females than in adult males. The other protein (CBG) bound both [3-H]cortisol and [3-H]progesterone. Binding of these compounds could be inhibited by unlabeled cortisol and progesterone, but not by unlabeled 5 alpha DHT, testosterone, or E2. CBG had a sedimentation of congruent to 3.9 S and an apparent molecular weight of congruent to 105,000. TeBG could be separated from CBG by a 60% ammonium sulfate precipitation and by gel filtration chromatography. Both proteins are thermolabile; TeBG is inactivated at temperatures above 30 degrees C and CBG is inactivated at temperatures above 50 degrees C.
Mol Cell Endocrinol 1975 May
PMID:Steroid-binding proteins in rabbit plasma: Separation of testosterone-binding globulin (TeBG) from corticosteroid-binding globulin (CBG), preliminary characterization of TeBG, and changes in TeBG concentration during sexual maturation. 4 21

Glycosaminoglycans (GG) were isolated from commercial Ateroid and compared with those from bovine duodenal mucosa and pancreas. The major GG in Ateroid is heparin. Heparan sulfate (HS) and dermatan sulfate were also found. HS, chondroitin sulfates, and heparin were isolated from duodenal mucosa after papain digestion, but a residue, non-digestible, was mostly heparin. Pancreas contains very little GG, and the GG composition is similar to that of mucosa. The heparin isolated from Ateroid and mucosa have similar lipoprotein lipase-releasing activity, but the former has considerably less anticoagulant activity. Interestingly, papain digestion of mucosa and pancreas did not release all heparin from the tissue, suggesting that the protein to which heparin is linked is not readily accessible to the enzyme.
Mol Cell Biochem 1975 Sep 30
PMID:Glycosaminoglycans from Ateroid and bovine duodenal mucosa and pancreas. 5 31

The distribution of disulfide-groups was investigated in the tunica propria of human seminifersou tubules by means of a thiosulfation/Alcian Blue + 0.8 Mol MgCl2-staining reaction. Controls had shown the absence of significant amounts of sulfhydryl- or sulfate-groups in the lamina propria, which groups would also be demonstrated by the method employed. The lamina propria of human seminiferous tubules is rich in disulfide groups. The staining reaction decreases in the region of the tubulus rectus, is only faint in the connective tissue which underlies the epithelium of the rete testis, and is absent in the lamina propria of efferent ducts. It is suggested that microfibrils and type IV collagen (both rich in cystine) are the materials responsible for the histochemical reaction described. The occurrence of multiple layers of basal lamina material (type IV collagen) and bundles of microfibrils is shown in comparative electron microscopic studies.
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PMID:Histochemical demonstration of disulfide-groups in the lamina propria of human seminiferous tubules. 7 13

Testosterone-estradiol binding globulin (TeBG) is known to change in various endocrinological environments such as estrogen administration, pregnancy and aging. Several methods, including dextran coated charcoal, equilibrium dialysis and ammonium sulfate precipitation, were used to measure the binding capacity of TeBG, but these were not simple and accurate. We therefore measured TeBG levels in human serum by means of a steady state polyacrylamide gel electrophoresis and found that this method was simple and accurate for the determination of the binding capacity of TeBG. The value of TeBG in normal adults (27 approximately 32 years old) was 3.88 +/- 0.45 x 10(-8) Mol and in patients with benign prostatic hypertrophy the value was high (5.49 +/- 1.35 x 10(-8) Mol compared to that of normal adults.
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PMID:[A steady state polyacrylamide gel electrophoresis for the determination of testosterone-estradiol binding globulin (author's transl)]. 8 59

Bio-Gel A-5m chromatography has been used to separate apparent multiple forms of cyclic nucleotide phosphodiesterase from rat erythrocytes. Cyclic AMP phosphodiesterase was resolved by gel filtration into three peaks of activity with apparent molecular weights of about 300,000, 225,000 and 100,000, while cyclic GMP phosphodiesterase activity in gel column fractions was too low to permit meaningful estimates of its molecular weight. All three of the separated peaks of cyclic AMP phosphodiesterase activity displayed anomalous kinetic behaviour suggestive of negative cooperativity. The possibility that multiple phosphodiesterase activities could arise from in vitro alterations of a single enzyme was investigated. Similar changes in gel filtration profiles resulted when erythrocyte extracts were treated with trypsin or ammonium sulfate or were incubated at 37 degrees C. After these treatments, a large proportion of the enzyme activity occurred in low (ca. 100,000) molecular weight regions. The low molecular weight phosphodiesterase activities from untreated, incubated, and trypsin-treated extracts possessed similar properties. All were inhibited by methylxanthines, had pH optima of approximately 8.0, and similar kinetic properties and requirements for divalent cations. These observations raise the possibility that preparative procedures or limited proteolysis occurring during preparation and handling of extracts can contribute to the apparent multiplicity of enzyme forms seen after gel filtration of phosphodiesterase from rat erythrocytes and perhaps other cell types.
Mol Cell Endocrinol
PMID:Apparent multiple forms of cyclic AMP phosphodiesterase from rat erythrocytes. 18 74

Cytochrome c oxidase from the inner membrane of yeast mitochondria consists of seven nonidentical protein subunits, three being synthesized on mitochondrial ribosomes (molecular weights I: 43 K, II: 34 K, and III: 24 K) and four being made on cytoplasmic ribosomes (molecular weights IV: 14 K, V: 12 K, VI: 12 K, and VII: 4.5 K). In the present study all four cytoplasmically synthesized subunits of the enzyme were isolated on a large scale using ion exchange chromatography and gel filtration. Their amino acid composition as well as their amino- and carbosy-terminal amino acid residues have been determined. Sequence determinations of subunits IV and VI are already in an advanced state. The sequence of subunit VI is characterized by a large amino-terminal stretch dominated by charged amino acid residues followed by a cluster of hydrophobic amino acids. The binding site of yeast cytochrome oxidase for cytochrome c was studied by chemical crosslinking experiments. The formation of a disulfide bridge between the two proteins was observed by using cytochrome c from yeast modified with 5-thionitrobenzoate at the cysteinyl residue in position 107. Alternatively, a disulfide between yeast cytochrome c and the oxidase could be formed directly by oxidation with copper phenanthroline. Gel electrophoresis of the crosslinked complexes in sodium dodecyl sulfate revealed a new protein band with an apparent molecular weight of 38 K. This new band appears to be derived from cytochrome c and from subunit III of cytochrome oxidase.
Mol Cell Biochem 1977 Feb 04
PMID:Structure of cytochrome c oxidase from baker's yeast - a progress report. Preparation of four subunits for amino acid sequence determination and attempts to localize the cytochrome c binding site. 19 98

In Saccharomyces cerevisiae, the products of eleven different genes are needed for a functional sulfate assimilation pathway. Only five enzymatic steps are known in this pathway. The study of the gene-enzyme relationships has shown that the enzymes catalysing two of these steps are probably heteropolymeric. Moreover, mutations in three unlinked genes lead to multiple enzymatic losses. Different hypotheses are made to account for these results.
Mol Gen Genet 1977 Jul 07
PMID:Methionine biosynthesis in Saccharomyces cerevisiae. II. Gene-enzyme relationships in the sulfate assimilation pathway. 19 88

In Saccharomyces cerevisiae, argB and argC define two adjacent and complementing loci, with mutants defective in two consecutive steps of arginine biosynthesis: N-acetylglutamate kinase (AG-kinase) and N-acetylglutamyl-phosphate reductase (AGPreductase). These enzymic activities are readily separated by ammonium sulfate fractionation or Sephadex G-200 chromatography. This suggests that each activity is carried in vivo by a different protein. The synthesis of the two enzymes is coordinately regulated, with an 85-fold difference in specific activities between fully repressed and fully derepressed cells. Missence mutations of the argB locus are defective in AGkinase only. Nonsense mutations in the argB locus are defective in both activities. Missense and nonsense mutations in the argC locus are defective in AGPreductase, with a few alleles also showing a reduced level of AGkinase. These data are best explained by assuming that argB and argC are two genes transcribed as a single messenger from argB to argC. This messenger produces in vivo two distinct proteins corresponding to the argB and argC gene products, either because translation can be initiated at the beginning of both genes, or because a large polypeptide is specifically cut in vivo to yield the gene products of argB and argC.
Mol Gen Genet 1979 Jan 11
PMID:Organization and expression of a two-gene cluster in the arginine biosynthesis of Saccharomyces cerevisiae. 22 May 8


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