Studies of nucleotide sequences in TMV-RNA. II - The action of spleen diesterase
Spleen diesterase action on polynucleotide and ribonucleic acid infectivity
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Spleen diesterase action on polynucleotide and ribonucleic acid infectivity
Optical properties, fluorescence, and absorption spectra of reduced nicotinamide adenine dinucleotide
Photometric method based on the use of bacterial luminiscent reaction quantitatively detects the presence of flavin compounds in all forms of life. Aqueous cellular dispersion of a biological sample with an aqueous perchloric acid ruptures the cells and frees the flavin coenzymes from their proteins.
Mechanism of DNA repair of radiation injury and survival properties of cells under conditions of normal growth, starvation, and DNP treated
Flavoprotein/cytochrome b/559/ role as branch of Halobacterium electron transport in DPNH oxidase determined by salt dependence of reduced DPNH
The isozymes considered are designated 'liver type' and 'muscle type' based on the tissue of highest concentration. Electrophoretic analysis shows that the liver type is found in small amounts or is undetectable in all tissues studied except liver. The muscle type is found in skeletal muscles and kidney. Presumptive hybrid enzymes occur at low levels in chicken liver and kidney. The tissue distribution of glyceron-3-P dehydrogenase in several birds capable of sustained flight is different than in chicken.
Nucleoside 5'-polyphosphates (N5PP) formed when solutions of nucleoside 5'-phosphates (N5P) and trimetaphosphate (TMP) are dessicated at room temperature are studied by paper chromatography, electrophoresis, and metal catalytic reactions. Divalent Mg ion exhibited superior catalytic function to other divalent metal ions in the reaction. Major reaction products are indicated. The importance of the N5PP series, TMP, and N5-triphosphate as substrates of RNA and DNA synthesis, and under postulated prebiotic conditions likely to obtain during prebiological ages of the earth, is emphasized and discussed. Alternate drying and wetting, evaporation from a prebiotic puddle, concentration of solubles in the remaining liquid phase, metal catalysis, and the role of these substances in the formation of amino acids and long-chain polyphosphates are considered.
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The primary sequence of the 5S ribosomal RNA isolated from the free-living bioluminescent marine bacterium Beneckea harveyi is reported and discussed in regard to indications of phylogenetic relationships with the bacteria Escherichia coli and Photobacterium phosphoreum. Sequences were determined for oligonucleotide products generated by digestion with ribonuclease T1, pancreatic ribonuclease and ribonuclease T2. The presence of heterogeneity is indicated for two sites. The B. harveyi sequence can be arranged into the same four helix secondary structures as E. coli and other prokaryotic 5S rRNAs. Examination of the 5S-RNS sequences of the three bacteria indicates that B. harveyi and P. phosphoreum are specifically related and share a common ancestor which diverged from an ancestor of E. coli at a somewhat earlier time, consistent with previous studies.
The potential of diiminosuccinonitrile (DISN) as a prebiotic phosphorylating agent is studied. This compound is formed readily by the oxidation of diaminomaleonitrile, a tetramer of HCN. DISN is shown to produce the cyclization of 3'-adenosine monophosphate to adenosine 2',3'-cyclic phosphate in up to 40 percent yield. The DISN-mediated phosphorylation of uridine to uridine monophosphate is determined not to proceed efficiently in aqueous solution. The reaction of DISN and BrCN with uridine-5'-phosphate and uridine is found to result in the formation of 2,2'-anhydronucleotides and 2,2'-anhydronucleosides, respectively, and other reaction products resulting from an initial reaction at the 2' and 3'-hydroxyl groups. Homoionic montmorillonites were employed to study the clay mineral catalysis of the cyclization of adenosine-3'-phosphate.
Diminosuccinonitrile (DISN), formed by the oxidation of diaminomaleonitrile, has been investigated as a potential prebiotic phosphorylating agent. DISN affects the cyclization of 3'-adenosine monophosphate to adenosine 2',3'-cyclic phosphate in up to 39 percent yield. The mechanism of this reaction was investigated. The DISN-mediated phosphorylation of uridine to uridine monophosphate does not proceed efficiencly in aqueous solution. The reaction of DISN with uridine-5'-phosphate and uridine results in the formation of 2,2'-anhydronucleotides and 2,2'-anhydronucleosides respectively, and other reaction products resulting from an initial reaction at the 2'- and 3'-hydroxyl groups. The clay mineral catalysis of the cyclization of adenosine-3'-phosphate was investigated using homoionic montmorillonites.
In the present paper, a report is presented on the effect of pH and carbonate on the hydrolysis rate constants of N-blocked and free aminoacyl adenylate anhydrides. Whereas the hydrolysis of free aminoacyl adenylates seems principally catalyzed by OH(-), the hydrolysis of the N-blocked species is also catalyzed by H(+), giving this compound a U-shaped hydrolysis vs. pH curve. Furthermore, at pH's less than 8, carbonate has an extreme catalytic effect on the hydrolysis of free aminoacyl-AMP anhydride, but essentially no effect on the hydrolysis of N-blocked aminoacyl-AMP anhydride. Furthermore, the N-blocked aminoacyl-AMP anhydride is a very efficient generator of peptides using free glycine as acceptor. The possible significance of the observations to prebiological peptide synthesis is discussed.
The directed synthesis of biopolymers in an abiotic environment is presumably a cyclic sequence of steps which may be realized in a fluctuating environment such as a prebiotic pond undergoing wetting-drying cycles. Soluble mineral salts have been proposed as an essential component of this fluctuating environment. The following sequence may be considered as a most primitive mechanism of information transfer in a fluctuating environment: (1) adsorption of a biomolecule onto a soluable mineral salt surface to act as an adsorbed template; (2) specific adsorption of biomonomers onto the adsorbed template; (3) condensation of the adsorbed biomonomers; and (4) desorption of the elongated oligomer. In this investigation, the salts selected for study were CaSO4.2H2O(gypsum), SrSO4, and several other metal sulfates and chlorides. Adsorption of the monomeric species, gly, 5'AMP 5'GMP, and 5'CMP was investigated. The adsorbed template biopolymers used were Poly-A, Poly-G, Poly-C, and Poly-U. The results of studies involving these experimental participants, the first two steps of the proposed primitive information transfer mechanism, and condensation of amino acids to form oligomers in a fluctuating environment are to be reported.
Examples of chiral selection in nonenzymatic aminoacylation of internal 2-prime hydroxyl groups of oligo- and polynucleotides are discussed as an evidence for the early evolution of bionucleotides. Some factors that could influence the degree of this chiral selection and its direction are discussed. These include the structure of the aminoacyl component, the structure of the nucleoside component, and the reaction conditions. Investigation of the mechanism of this reaction was aided by the use of 3-prime inosine methyl phosphate (as a simplified model for a dinucleoside monophosphate) and proton NMR spectroscopy of t-butoxycarbonyl-alanyl esters of nucleosides as models for the transition state of the aminoacylation reaction itself.
Bismonophosphoimidazolides of acyclic analogues of guanosine IV and adenosine V were synthesized. They undergo oligomerization in the presence of complementary polynucleotide templates. Details of their synthesis and their subsequent template- and nontemplate-directed reactions are described, and their possible relevance to the origin of life is discussed.
The nucleoamino acids 1-(3'-amino,3'-carboxypropyl)uracil (3) and 9-(3'-amino,3'-carboxypropyl)adenine (4) have been prepared as (L)-en-antiomers and as racemic mixtures. When 3 or 4 is suspended in water and treated with N,N'-carbon-yldiimidazole, peptides are formed in good yield. The products formed from the (L)-enantiomers are hydrolyzed to the monomeric amino acids by pronase. Attempts to improve the efficiency of these oligomerizations by including a polyuridylate template in the reaction mixture were not successful. Similarly, oligomers derived from the (L)-enantiomer of 3 did not act as templates to facilitate the oligomerization of 4.