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)

Compounds were studied that inhibit the oxidative degradation of human serum albumin by peroxidase and the enzyme model, iron hydroxide. Differences between the two oxidants gave clues for the mechanism of inhibition. The inhibitors studied were inorganic anions, phosphate, sulfate, carbonate and molybdate; organic anions, decanoate and glycocholate; and the nonionic species, glycogen. Such inhibitors might be considered as adjuvants in senescence: by decreasing the rate of enzymic oxidation of essential body proteins, they would, in the course of aging, reduce some of the physiological changes occurring as a result of accumulation of degraded protein.
Mol Biol Rep 1979 Feb 15
PMID:Inhibitors of oxidative degradation of protein: gerontological implications. 44 Feb 99

The kinetics of self-association for beef liver glutamate dehydrogenase (EC 1.4.1.3) have been measured by using pressure perturbation in both the time domain and the frequency domain by monitoring scattered light intensity. The kinetic behavior is entirely consistent with the random self-association model proposed by Thusius et al. [Thusius, D., Dessen, P., & Jallon, J. M. (1975) J. Mol. Biol. 92, 413--432]. The activation volume deltaV for association is estimated to be positive, and it is shown that this provides further corroboration of the molecular mechanism advanced by these same authors. A rapid shift in scattered light intensity is attributed to preferential interaction between the phosphate anion and the protein, proceeding with a positive volume change (2--5 mL/mol of phosphate). A description of the instrument developed for this study is also included.
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PMID:Relaxation kinetics of glutamate dehydrogenase self-association by pressure perturbation. 44 70

When peripheral lymphocytes stimulated with phytohemagglutinin were permeabilized in vitro, (3H) dCTP acted as a precursor for DNA synthesis, but the formation of a compound soluble in organic solvents could also be demonstrated. The structure of the latter compound was studied analyzing the products formed after alkaline hydrolysis or an enzymatic treatment with nucleotide pyrophosphatase. Both treatments led to the formation of (3H)dCMP. When stimulated lymphocytes were labeled in vivo with (14C)glycerol before permeabilization and ulterior labeling with (3H)dCTP a double labeled compound was obtained. When this compound was submitted to alkaline hydrolysis, (3H)dCMP and (14C)glycerol-3-phosphate were obtained. It was concluded that the compound soluble in organic solvents was phosphatidyl-dCMP.
Mol Cell Biochem 1979 Apr 02
PMID:Synthesis of phosphatidly-dCMP in permeabilized normal human lymphocytes. 46 Jan 75

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

A model of the molecular mechanism of tobacco mosaic virus (TMV) assembly in vitro is proposed. The model is based on the assumption that on interaction of TMV RNA chain with a double protein disk two different types of structural alterations occur in the protein subunits: "dislocating alterations" leading to screw dislocation of the disk into a helix fragment and "locking alterations" leading to locking of the RNA chain between the subunits layers. During initiation of TMV assembly the dislocating alterations occur cooperatively in all subunits of the disk as a result of specific interaction of purines (guanines) in the middle (horizontal) position of every trinucleotide unit with the 32--39 loop of the TMV protein molecule. Locking alterations are induced non-cooperatively by phosphate groups and lateral (vertical) bases of trinucleotide units. The sequence of events during TMV assembly in vitro and the role of topological factors in this process are discussed.
Mol Biol (Mosk)
PMID:[Model for tobacco mosaic virus assembly in vitro: specific dislocation by cooperative single-letter purine recognition and non-cooperative RNA "locking" between subunit layers]. 47 Sep 37

By the interaction of pyridoxamine- and pyridoxale-5'-thiophosphate with aspartate-aminotransferase complexes similar in their properties to corresponding forms of the native enzyme were obtained. Reversible convertions of the obtained complexes were performed by short time incubation with substrates. It was found that the thioester bond can be splitted as a result of incubation of the pyridoxamine-5'-thiophosphate form of the enzyme with the substrate mixture for several hours at pH 5.0. The same split took place during incubations of the complex of apo-enzyme with L-Nalpha-(pyridoxyl-5'-thiophosphate)-glutamic acid at pH 3.5 within several minutes. The split of the thioester bond was accomplished by formation of phosphate-enzyme bonds, the latter was found to be stable towards gel-filtration and denaturation, but unstable to proteolysis. The labilisation of the thiophosphate bond was explained in terms of changes of structure and specificity of the anchoring site of 5'-phosphoryl group according to the reaction coordinate.
Mol Biol (Mosk)
PMID:[Reaction of apo-aspartate aminotransferase with 5-thiophosphate analogues of the coenzyme. Split of the thiophosphate bond]. 47 Sep 45

Ecdysone 20-monooxygenase, the enzyme system that hydroxylates ecdysone at C-20 of the side-chain to form ecdysterone, has been characterized in the fat body of early last instar larvae of the tobacco hornworm, Manduca sexta, using a radioenzymological assay. Ecdysterone was demonstrated to be the product of the enzyme system by high-pressure liquid chromatography, gas-liquid chromatography and mass spectrometry. Differential centrifugation, sucrose-gradient centrifugation, electron microscopy and organelle-marker enzyme analysis revealed that ecdysone 20-monooxygenase activity is associated with the mitochondria. The enzymatic properties of ecdysone 20-monooxygenase are that it is most active in a 0.05 M phosphate buffer, is inhibited by Mg2+ and exhibits pH and temperature optima at 7.5 and 30 degrees C, respectively. The enzyme complex has an apparent Km for ecdysone of 1.60 x 10(-7) M and is competitively inhibited by its product, ecdysterone, with an apparent Ki of 2.72 x 10(-5) M. The cytochrome P-450 nature of this insect steroid hydroxylase was initially suggested by its obligate requirement for NADPH and its inhibition by carbon monoxide, p-chloromercuribenzoate, metyrapone and p-aminoglutethimide but not by cyanide. Difference spectroscopy revealed the presence of cytochrome P-450 in the fat-body mitochondrial fraction. A photochemical action spectrum of ecdysone 20-monooxygenase activity confirmed the involvement of cytochrome P-450 in this monooxygenase system.
Mol Cell Endocrinol 1979 Sep
PMID:Ecdysone 20-monooxygenase: characterization of an insect cytochrome p-450 dependent steroid hydroxylase. 48 26

The condensation products obtained from 0.01M S-glycyl-N-acetyl-cysteamine at different pH's were investigated. The highest yields of diketopiperazine (approx. 50%) were observed in phosphate buffers between pH 7.5 and 8.5. The highest yields of diglycine (46%), triglycine (10%) and tetraglycine (2%) were observed in carbonate buffers at pH 9.5. At pH 8.0, over 90% of the glycyl residues of 0.15M S-glycyl-N-acetylcysteamine were incorporated into condensation products, mainly DKP (60--70%). The yields of products from the condensation of S-glycyl-ethanethiol under similar conditions closely resembled those obtained with S-glycyl-N-acetylcysteamine.
J Mol Evol 1979 Oct
PMID:The formation of peptides from glycine thioesters. 50 43

On the basis of general stereochemical considerations the classification of the stacking state of dinucleoside phosphate (DNP) including eight types of stacks of nucleic bases has been suggested. With the use of the algorithm, which makes possible determination of the backbone conformation for the given nucleic bases arrangement, the stacking conformes of DNP were analysed by atom-atom potential method. For all compounds different types of stacking conformes were obtained with energy values lower than that for the unstacking state. It follows from the results of calculations that for description of the conformational situation of DNP in solution the "non-canonical" conformers should be born in mind. In particular the forms having different sugar conformations in Np- and in pN-parts of the dimers are of interest. The effect of choice of the atom-atom potential functions on optimal conformation of DNP is discussed. For single-stranded RNA several regular and non-regular structures are proposed.
Mol Biol (Mosk)
PMID:[Eight types of stacking interaction in dinucleotides. Conformational analysis of ApA, ApC, CpA, CpC, GpG]. 50 64

The formation of glycerol occurs when a solution of DL-glyceraldehyde is heated in the presence of hydrogen sulfide at room temperature. DL-glyceraldehyde and dihydroxyacetone treated with hydrazine, as well as DL-glyceraldehyde incubated with formaldehyde are also partially converted to glycerol. The yields of the above reactions are from approximately 1% to about 3%. The formation of glycerophosphates occurs when glycerol is heated with ammonium dihydrogen phosphate and either urea or cyanamide. The yield of glycerophosphates is about 30%, most of which is sn-glycero-1 (3)-phosphate. These findings indicate that glycerol and sn-glycero-3-phosphate, which are moieties of glycerolipids, could have been formed under conditions which may have prevailed on the primitive Earth.
J Mol Evol 1979 Dec
PMID:Cyanamide mediated synthesis under plausible primitive earth conditions. VI. The synthesis of glycerol and glycerophosphates. 53 3


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