The effect of tin chloride on the structure and function of dna in human white blood cells

Tin compounds are being used increasingly in

in industry and in medicine. There have been relatively few studi

ng term biological effects of this metal, although acute effects h

cumented. In this report we describe experiments which show tha

stannous chloride, is readily taken up by human white blood cells

an cause damage to DNA. Damage was detected in WBC after e

-50 μM tin(II) for 30 min at either 0°C or 37°C. The amount o

served was more extensive than that produced by exposure of

nolar amounts of chromium(VI), a known carcinogen and DNA

agent. Additional indication of cellular damage is that exposm

n lymphocytes or mouse splenocytes to tin(II) interfered with thei

o be stimulated by the polyvalent mitogen concanavalin A (Con A).

rast, tin(IV) was not taken up by cells, did not cause DNA damage nor d

inhibit stimulation of DNA synthesis in cells that were exposed to Con A.     

Nonenzymic hydrolysis of ATP–infrared investigations of intermolecular interactions

The nonenzymic hydrolysis of

and

were studied by infrared (IR) spectroscopy. Protons resulting from hydrolysis of ATP are not bound to the N₁ atoms of the adenine residues. With hydrolysis of

, these protons are partially bound to the terminal phosphate group of ADP, namely,

,

,

, and

, present after hydrolysis. With decreasing pH or when Mg²⁺ ions are present, all hydrolysis protons are attached to the orthophosphate molecules.With hydrolysis of

the pH decreases up to 40% degree of hydrolysis. Then the system becomes self-buffered in the physiological pH region. A similar pH decrease is found with hydrolysis of

. With these systems, however, the pH decreases slightly also at degrees of hydrolysis larger than 40%. No other systems show pronounced pH changes during hydrolysis; in other words, they are buffer systems.The IR bands demonstrate that mesomeric bond resonance in the phosphate groups strongly depends on whether protons are present at these groups. Regarding the equilibria of proton attachment mentioned above, mesomeric bond resonance in these groups strongly depends on pH and on the presence of

ions.With hydrolysis of ATP, two POH groups are formed that bind H₂O molecules via strong hydrogen bonds, changing the solvate structure. Finally, easily polarizable hydrogen bonds are formed, for instance,

bonds with the hydrolysis of

, and

bonds with the hydrolysis of

. These bonds strongly interact with their environment. The formation of these hydrogen bonds strongly depends on pH and the presence of

ions.All these effects, especially the intermolecular ones, contribute to the change of free energy during ATP hydrolysis.     

A survey of hydrogen bond geometries in the crystal structures of amino acids

An analysis of the geometries of the hydrogen bonds observed by neutron diffraction in thirt-two crystal structures of amino acids shows the following results. Of the 168 hydrogen bonds in the data set, 64 involve the zwitterion groups 

and $\text{C}$O₂. Another 18 are from

to sulphate or carbonyl oxygens. The majority, 46, of these

H … O bonds are three-centered (bifurcated). Nine are four-centered (trifurcated). The geometry in which the three-centered hydrogen bond involves both oxygens of the same carboxylate group is not especially favoured. When it does occur, one hydrogen bond is generally shorter and the other longer, than when the bonding involves oxygens on different carboxylate groups. The shortest hydrogen bonds are the OH … O $\text{C}$, from a carboxylic acid hydroxyl to a carboxylate oxygen, and NH … O$\text{C}$ when the nitrogen is the ring atom in histidine or proline. Carboxylate groups, on average, accept six hydrogen bonds, with no examples of less than four bonds. The reason for the large number of three-centered

H … O$\text{C}$ bonds is therefore a proton deficiency arising from the disparity between the tripled donor property of the

groups and the sextuple, on average, acceptor property of the carboxylate groups. There is good geometrical evidence for the existence of H … O and H … Cl^? hydrogen bonds, especially involving the hydrogen atoms on α-atoms.     

Carbohydrate binding activity of a lectin-like glycoprotein from stems and leaves of Dolichosbiflorus

A glycoprotein from the stems and leaves of the $\text{Dolichos}$$\text{biflorus}$ plant that cross reacts with antibodies to the seed lectin has been found to bind to affinity columns of blood group A + H substance covalently linked to Sepharose. This binding of the cross reactive material to the affinity resin differs from that of the seed lectin in that it is easily dissociated with 0.15 M NaCl. Affinity electrophoresis using entrapped blood group A + H substance shows that the carbohydrate binding activity of the cross reactive material is weakly inhibited with N-acetyl-D

-galactosamine and N-acetyl-D

-glucosamine. Glucose, mannose and galactose gave no inhibition when tested at concentrations of 50 mM. These data indicate that the specificity of the cross reactive material is somewhat different from the N-acetyl-D

-galactosamine specificity of the seed lectin. The significance of these findings is discussed in relation to the structural similarities of the cross reactive material and the seed lectin.     

Studies of the self-association of bacteriophage T4 gene 32 protein by equilibrium sedimentation.

The self-association of the bacteriophage T4 gene 32 protein has been examined in the analytical ultracentrifuge under varying conditions to determine the nature of the process. The process is not a simple indefinite association with one association constant (monomer

dimer

trimer

etc.). The complexity of the process is shown by (1) peculiarities in the molecular weight versus concentration curves, in the region of the dimer (observed with increasing ionic strength, at pH 10, in 0.04 m-MgCl₂, with aged preparations, at 19 °C and in the presence of the oligonucleotide d(pT)₁₀), (2) the increased sigmoidicity of the association curve in the presence of glycerol or oligo[d(pT)₄], and (3) the discontinuity in the association curve at the tetramer at a pH value of approximately 9.4. A model with two association constants which could vary independently (monomer

dimer

tetramer

etc.) explained many of the findings. However, a more complex model was required to explain curves which had a plateau at the dimer with increased association at higher protein concentrations. Thus, under all conditions examined there is evidence for more than one type of protein-protein interaction. These different interactions may be involved in a physiological function such as recombination.     

Genetic and sequence analysis of frameshift mutations induced by ICR-191

A genetic and sequence analysis of 373 ICR-191-induced mutations in the lacI gene of Escherichia coli reveals that 365 of the mutations (97·9%) are frameshifts involving the addition or deletion of a single

base-pair from a

sequence including, in one case, a

sequence. Some of the remaining eight mutations (2·1%) represent the loss or gain of a

base-pair from a

sequence. Certain mutational sites are relative hotspots for ICR-191-induced mutations, and we have analyzed the role of surrounding sequences on relative mutation rates. The preference for +1 frameshifts or ?1 frameshifts is site-specific, so that at some sites +1 frameshifts predominate by a 10:1 ratio, whereas at other sites ?1 frameshifts are favored by an approximately 2:1 ratio. The characterized frameshift mutations in lacI described here are useful for constructing systems to detect other frameshift and deletion mutations.     

A DNA sequence cleaved by restriction endonuclease R.EcoRI in only one strand.

Restriction endonuclease EcoRI cuts both strands of the DNA sequence

generating two separate frayed ends (Hedgpeth et al., 1972). Here it is shown that under standard digestion conditions, the enzyme also attacks the sequence

but cuts only one strand. The resulting nick is an efficient initiation point for DNA synthesis by Escherichia coli DNA polymerase I, allowing the selective labelling of one strand of the DNA duplex.In buffers of low molarity and high pH (8.5), EcoRI cleaves sequences with the form

(Polisky et al., 1975). Thus it seems that under both sets of conditions the enzyme recognises the four-base-pair core sequence

and that its ability to cleave different adjacent phosphodiester bonds varies with pH and ionic strength.     

Enzymic synthesis of 5-acetamido-9-azido-3,5,9-trideoxy-D-glycero-D-galacto-2-nonulosonic acid, a 9-azido-9-deoxy derivative of N-acetylneuraminic acid

N-Acetylneuraminate synthase from $\text{Neisseria meningitidis}$ 6OE catalyzes the conversion of phosphoenolpyruvate and 2-acetamido-6-azido-2,6-dideoxy-

-mannose into 5-acetamido-9-azido-3,5,9-trideoxy-

-$\text{glycero}$-

-$\text{galacto}$-2-nonulosonic acid. The product, a 9-azido-9-deoxy derivative of N-acetylneuraminic acid, is indistinguishable from a chemically synthesized sample by i. the thiobarbituric acid assay, ii. paper electrophoresis, and iii. paper electrophoresis following sodium borohydride reduction. Both the chemically and the enzymically synthesized samples are substrates of the reaction catalyzed by CTP:CMP-N-acetylneuraminate cytidylyl-transferase from $\text{Neisseria meningitidis}$ 6OE     

Reaction kinetics of P-700, cytochrome c-553 and cytochrome f in the cyanobacterium, Synechococcus sp

Absorption changes invoked by short flashes in the Soret band region were measured in the thermophilic cyanobacterium Synechococcus sp. and photoresponses of P-700, cytochrome c-553 and cytochrome f were resolved with the aid of a microcomputer. Cytochrome c-553 was oxidized very rapidly with a half-time of less than 20 μs, while the half oxidation time of cytochrome f was 35–45 μs. The two cytochromes were reduced monophasically with half-time of 2 ms after a lag lasting a few milliseconds. The reduction kinetics of P-700 showed three exponential phases with half-times of 40 μs, 200 μs and 2 ms, which are ascribed to electron donation from cytochrome f, the Rieske iron-sulfur protein and plastoquinone, respectively. The results support the following sequence and rates of linear electron transport at the physiological temperature of the cyanobacterium: P-700

cytochrome c-553

cytochrome f

Rieske protein

plastoquinone.     

A bicyclo-somatostatin analog,highly specific for the inhibition of growth hormone release

The tetradecapeptide somatostatin was cyclized by a combination of conventional and solid phase peptide synthesis methods, to a homodetic cyclic disulfide tetradecapeptide, Wy-40,391:

The analog inhibits the release of growth hormone (GH) $\text{in vivo}$ without affecting either insulin or glucagon secretion. A correlation between binding affinity to the receptors and specificity is suggested.     

Evidence for a convalent intermediate between alpha-glucosidase and glucose

A stable enzyme-glucose intermediate has been obtained in the short-term reaction between α-methyl-

-glucosidase and α-methyl-

-¹⁴C-glucopyranoside. A rapid-flow technique was employed in which phenol was used to terminate the reaction and to trap the product. It is believed that a covalent linkage is involved because (a) continued washing of the denatured protein failed to remove the radioactivity and (b) the radioactivity was retained by a tryptic peptide isolated by gel filtration. Treatment of the labeled protein with 2 $\text{N}$ HCl at room temperature released over 80% of the radioactivity as a compound with the same chromatographic mobility as glucose. No radioactive product was formed when bovine serum albumin replaced the enzyme, nor when glucosylamine, a potent glucosidase inhibitor, was present with the enzyme.     

The nucleotide sequence of 4.5 S rRNA from tomato chloroplasts

The nucleotide sequence of 4.5 S rRNA from tomato (Lycopersicum esculentum Mill) chloroplasts has been determined to be:

. The 4.5 S rRNA is 103 nucleotides long and has a free 5′-terminal hydroxyl group. It shows at high degree of homology with chloroplast 4.5 S rRNA from other plants.     

The synthesis of some polyether bridged diphosphines and their reaction with Rh(COD)acac

The polyether bridged diphosphines,

(n = 1,2) have been prepared in 60–70% yield by reduction of the corresponding diphosphinedioxides with Si₂Cl₆ or (i-Bu)₂AlH. These diphosphinedioxides have been prepared in 75–90% yield by reaction of two equivalents of the appropriate

with one equivalent of di- and triethylene glycol ditosylate.In general, reaction between the diphosphines, Rh(COD)acac and HClO₄ gives a mixture of species, cis-[Rh(COD)($\text{PP}$)] [ClO₄] being the main complex. This complex reacts with CO to η³-trans- [$\text{Rh(CO)(}\text{PO}$$\text{P}$)] [ClO₄].     

Structural Architecture of the Nucleosome Remodeler ISWI Determined from Cross-Linking,Mass Spectrometry,SAXS, and Modeling

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Variation in Activity State,Axonal Projection,and Position Define the Transcriptional Identity of Individual Neocortical Projection Neurons

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Increasing rigor in NMR-based metabolomics through validated and open source tools

Opportunities and challenges ahead for NMR-based metabolomics.

     

Structure of the Mitochondrial Aminolevulinic Acid Synthase,a Key Heme Biosynthetic Enzyme

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Discovery of the First Germline-Restricted Gene by Subtractive Transcriptomic Analysis in the Zebra Finch,Taeniopygia guttata

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