Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mitochondrial glycerol-3-P dehydrogenase (EC 1.1.99.5) has been purified in 20% yield from both rabbit skeletal muscle and brain using a four step procedure involving osmotic shock, solubilization with Triton X-100, hydrophobic chromatography, gel filtration, and preparative column isoelectrofocusing. The active muscle and brain enzymes were found to be 95% and 80% homogeneous, respectively. Final purification was performed on the denatured subunit. The active enzyme from each of the tissues focused at pH 5.25 +/- 0.12 and each produced similar biphasic thermal inactivation plots at 50 degrees C. Mixtures of the purified brain and muscle enzymes co-migrated in discontinuous electrophoresis gels and each enzyme exhibited a single polypeptide component on sodium dodecyl sulfate (SDS) gels either when run separately or in mixtures. The subunit molecular weight was shown to be 76,000 +/- 3,000 by SDS-gel electrophoresis and gel filtration in 6 M guanidine HCl. One mole of noncovalently bound FAD and 1 mole of iron were measured per Mr = 100,000. The amino acid composition was determined based on the assumption of 70 aspartate residues per subunit to give a Mr = 76,000. The absorption spectrum has a maximum at 416 nm and a shoulder at 450 to 460 nm which is bleached on treatment with sodium dithionite. The maximum at 416 nm is removed by treatment with mersalyl.
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PMID:Isolation and characterization of flavin-linked glycerol-3-phosphate dehydrogenase from rabbit skeletal muscle mitochondria and comparison with the enzyme from rabbit brain. 70 Dec 95

1. A superoxide dismutase [EC 1.15.1.1] was purified about 275-fold with a yield of 34% from Mycobacterium tuberculosis, strain H37Ra (attenuated strain), grown on a Sauton medium for two months. The purified enzyme was homogeneous as judged by polyacrylamide gel electrophoresis, and by analytical ultracentrifugation and sedimentation equilibrium studies. 2. The molecular weight of the enzyme was estimated to be approximately 88,000 by sedimentation equilibrium analysis. Since the molecular weight of the subunit was 21,000 as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis, the enzyme appears to be composed of four subunits of equal size. 3. Electron spin resonance (ESR) spectra showed that the enzyme contained ferric iron, and metal analysis showed that the enzyme contained ferric iron, and metal analysis showed that approximately 3.7 atoms of iron were present per mole of the enzyme, indicating the occurrence of 1 atom of iron per subunit. 4. The amino acid composition was apparently similar to those of the iron-containing superoxide dismutases from Escherichia coli, luminous bacteria, Pseudomonas ovalis, and blue-green alga. 5. Antibodies against the enzyme were raised in rabbits and immunological studies were performed. The enzyme from M. tuberculosis, strain H37Rv (virulent strain), was found to have antigenic structures identical with those of the H37Ra enzyme. On the other hand, the manganese-containing superoxide dismutases from other species of mycobacteria, i.e., Mycobacterium species, strain Takeo, M. phlei and M. lepraemurium, showed only partial immunological identity with the H37Ra enzyme. 6. During the growth of M. tuberculosis, strain H37Ra, the enzyme was found to be secreted into the culture medium.
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PMID:Superoxide dismutase from Mycobacterium tuberculosis. 82 61

A radioimmunoassay was developed for murine lactoferrin (LF), a non-heme, iron-binding glycoprotein which appears to be a specific biochemical marker of differentiation in several cell types. Lactoferrin was labeled with 125I by the chloramine-T method to yield a product having 20 muCi/mug protein and an isotope incorporation of 0.6 atoms of 125I per molecule. Separation of bound and free lactoferrin was accomplished by either of two procedures, a double-antibody technique or precipitation in the presence of 50% saturated ammonium sulfate. The entire assay, including counting, was accomplished in less than 2 days and had a lower limit of sensitivity and a range of 1 ng/ml and 1-32 ng/ml, respectively, using rabbit antiserum in a dilution of about 1:10,000. The binding between LF and rabbit antiserum exhibited two association constants having values of 1.8 x 10(11) and 1 x 10(9) l/mole. The assay was specific for lactoferrin and no cross-reactivity was observed with transferrin, a similar non-heme, iron-binding glycoprotein. Human lactoferrin specifically reacted with anti-mouse lactoferrin, but the binding was approximately 8000 times weaker than observed with mouse lactoferrin. Values for lactoferrin in milk and bone marrow granulocytes were obtained which agreed with levels obtained using other methods.
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PMID:Radioimmunoassay for murine lactoferrin, a protein marker of myeloid and mammary epithelial secretory cell differentiation. 83 25

Overall stability constants of mono-, bis-, and tris(pyrrolidone-k-hydroxamato)iron(III) chelates were determined in aqueous solutions at 25 degrees as log beta1=1.49, log beta11=1.55, and log betaIII=0.21, respectively, where beta1=[Fe(C5H7O3N2)2+][H+]/[F=E3+][HC5H7O3N2], betaII=[Fe(C5H7O3N2)2+][H+]2/[Fe3+][hc5h7o3n2]2, and betaIII=[Fe(C5H7O3N2)3][H+]3/[Fe3+][HC5H7O3N2]3. Stability constants of all three chelates were determined potentiometrically in the 3.00-3.23 pH region. The stability constant of the mono chelate also was determined spectrophotometrically at 25 degrees as log beta1-1.52 by measuring absorbance at 500 nm (absorbance maximum), where the molar absorptivity was epsilon=1124 liters/(mole cm). Biological implications of hydroxamic acid-containing compounds are discussed.
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PMID:Stability of (pyrrolidone-5-hydroxamato)iron (III) chelates. 84 96

A 21-year-old man had blue rubber bleb nevus syndrome: 1) hemangiomas of the skin all over the body; 2) hemangiomas of the digestive system; 3) iron-deficiency anemia. A giant mass of hemangiomas in the tranverse colon was resected surgically.
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PMID:Blue rubber bleb nevus syndrome: report of a case. 87 12

The purification of Methanobacterium thermoautotrophicum from a culture contaminated with a heterotrophic organism is described. A defined inorganic medium under H2/CO2 (80:20 v/v) has been developed to support growth of M. thermoautotrophicum up to a concentration of at least 1.7 g dry weight/l. In a conventional medium iron and nitrogen sources were found to be growth-limiting factors. Throughout most of the culture period the rate of transfer of hydrogen or carbon dioxide from gas to liquid was the factor which controlled the growth rate. The growth yields of bacteria were in the range of 0.6-1.6 g dry weight/mole CH4.
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PMID:Nutrition and factors limiting the growth of a methanogenic bacterium (Methanobacterium thermoautotrophicum). 88 84

We have isolated an iron-sulfur proteins from a Pseudomonas species grown on glucose. This protein has different properties from the two known iron-sulfur proteins isolated from other Pseudomonas species: rubredoxin and putidaredoxin. The iron-sulfur protein was purified to homogeneity by DEAE-cellulose column chromatography and Sephadex G-75 gel filtration. The absorption spectrum of the oxidized iron-sulfur protein shows a peak at 283 nm with shoulders at about 290, 320, and 410 nm. The protein contains 4 g atoms of iron and 4 moles of labile sulfur per mole of protein, and has a molecular weight of approximately 14,000. The amino acid composition of the protein shows a predominance of acidic amino acids. The Pseudomonas protein was found to be active for both photosynthetic nicotinamide nucleotide reduction by chloroplasts and cytochrome c reduction by spinach ferredoxin-NADP+ reductase [EC 1.6.7.1]. On the basis of these results, this protein appears to be unique among all known ferredoxins. From an evolutionary point of view, it appears to be more closely related to Azotobacter ferredoxin than to Desulfovibrio ferredoxin.
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PMID:Purification and properties of a four iron-four sulfur protein from a Pseudomonas species. 95 44

The isolation method and some peoperties of purple sulphur bacteria (Thiocapsa roseopersicina strain BBS) hydrogenase are described Hydrogenase molecular weight is found to be 66000; it contains 3.7 moles of S2- and 3.9 moles of Fe2+ per one mole of the enzyme;pI=4.2. The enzyme absorption spectrum has the maximum at 400-412 nm which is characteristic of proteins containing non-haem iron. Hydrogenase is suggested to consist pf 4 subunits of two types: with molar weight 27000 and 6000. Unlike other hydrogenases, this enzyme is rather resistant to O2 and is more thermostable: the inactivation of the enzyme was observed at the temperature above 80 degrees C; Hydrogenase preparation catalyses D2-H2O exchange reaction, H2 evolution from the reduced methyl viologene (MV) and H2 absorption in the presense of MV or benzylviologene but not in the presense of NAD(P), FAD, FMN, azocarmine, methylene blue and ferricyanide.
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PMID:[Purification and properties of hydrogenase from phototrophic bacterium Thiocapsa roseopersicina]. 102 87

The aging process has been studied by 0.09, 0.28 and 0.48 wt% iron added gold-10 wt% platinum alloys. The results obtained are as follows: (1) From the isochronal and isothermal aging, the electrical resistances decreased in proportion to increasing of iron. These decreases are occured to be ordered of iron and platinum. (2) The electrical resistances in the isochronal aging curves are minimized at limited temperature of 600 degrees approximately 680 degrees C, and the growth of nodules would be saturated at this temperature. (3) The apparent activation energies of aging process of Au-Pt-Fe alloys (0.09, 0.28 and 0.48 wt% Fe) were in the range of about 37 approximately 44 Kcal/mole. (4) In the results of the images atructure of nodules was lamella of fcc FePt3 phase and Au-Pt solid solution phase.
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PMID:[Age-hardening of minor amounts of iron added Au-10% Pt alloy (Part II) (author's transl)]. 106 27

The two 5-aminolevulinic acid synthetases of Rhodopseudomonas spheroides Y. were extracted from cells grown in a 'low-iron' medium and purified. They have a specific activity 10-fold higher than the 'high-iron' enzymes described by us previously and have the same properties except that they do not contain any iron and have one free-SH group more per mole of enzyme (2 for E1; , for E2) Their inhibition by adenosine triphosphate and iron and their oxidation-reduction sensitivity are discussed in terms of light, oxygen and heme feed-back regulation of bacteriochlorophyll sunthesis.
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PMID:5-Aminolevulinic-acid synthetases from Rhodopseudomonas spheroides Y. Comparison of the purification and properties of enzymes extracted from bacteria grown in different iron concentrations. 108 46


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