Regional chemotherapy of liver tumors

In the absence of adequate autogenous vein for tibial artery bypass in limb salvage surgery, the use of prosthetic grafts with a distal anastomotic vein cuff or patch has shown promising results. Here, we describe how the Florester Internal Vessel Occluder (Meadox UK, Bedfordshire, UK) can facilitate the construction of a distal anastomotic vein cuff.     

Quantitative determination of non-defect unstable structures in PVC through selective nucleophilic substitution with C6H5SNa

Summary The nucleophilic substitution with C₆H₅SNa, at -30°C, is compared for five PVC samples with various contents of isotactic triads. The conversion curves consist of a very fast stage followed by a steady one. All the samples are found to behave in the same way except for the content of the structures involved in the fast period. This content is estimated by extrapolating the straight lines of the steady stages to zero time. The obtained values are found to be a linear function of the content of isotactic triads. The results, together with some earlier ones, allow for the content of the labile non-defect structures in PVC to be determined.     

Mechanical improvement of hydroxyapatite by TiO<Subscript><Emphasis Type="Italic">x</Emphasis></Subscript> nanoparticles deposition

Deposition of Ti was carried out by laser ablation onto hydroxyapatite porous discs in an Ar atmosphere. Ti nanoparticles were deposited onto HAp surface in order to modify its roughness and morphology as it is observed by scanning electron microscopy (SEM) and scanning probe microscopy (SPM). A homogeneous distribution of Ti over the disc surface was corroborated by elemental mapping. A comparison of the hydroxyapatite hardness before and after deposition was performed using SPM nanoindentation. Transmission Electron Microscopy (TEM) showed that the Ti nanoparticles obtained were covered by an oxygen shell. It is shown that surface modifications of the covered HAp by Ti result in better mechanical properties, reducing the possible damage to the HAp ceramic by friction or impacts as it often happens in meniscus, bone junctions and the inclusion of prosthesis for human treatments.     

Synthesis and release of ATP by soluble mitochondrial F1 in complex with its inhibitor protein during dimethylsulfoxide-water transitions

Soluble mitochondrial F1 and F1 in complex with the natural ATPase inhibitor protein (F1-IP) catalyze the spontaneous synthesis of [gamma-32P]ATP from medium [32P]phosphate and enzyme-bound ADP when incubated in media with dimethylsulfoxide (Me2SO); under these conditions, the synthesized [gamma-32P]ATP is not released into the media, it remains tightly bound to the enzymes [Gómez-Puyou, A., Tuena de Gómez-Puyou, M. & de Meis, L. (1986) Eur. J. Biochem. 159, 133-140]. Some of the characteristics of the synthesized [gamma-32P]ATP were studied in F1 and F1-IP (ATPase activities of 70 and 1-3 micromol x min(-1) x mg(-1), respectively). In Me2SO media, gamma-phosphate of synthesized ATP in F1 or F1-IP exchanges with medium phosphate. From the rates of the exchange reaction, the half-times for hydrolysis of the synthesized ATP in F1 and F1-IP were calculated: 45 min and 58 min for F1 and F1-IP, respectively. The course that synthesized [gamma-32P]ATP follows after dilution of the Me2SO synthetic mixture with aqueous buffer was determined. After dilution, the half-life of synthesized ATP in F1 was less than 1 min. In F1-IP, ATP was also hydrolyzed, but at significantly lower rates. In F1-IP, dilution also produced release of the synthesized [gamma-32P]ATP. This was assayed by the accessibility of [gamma-32P]ATP to hexokinase. About 25% of [gamma-32P]ATP synthesized in F1-IP, but not in F1, was released into the media after dilution with aqueous buffer that contained 20 mM phosphate. Release of tightly bound ATP required the binding energy of phosphate and solvation of F1-IP, however, the particular kinetics of F1-IP were also central for medium ATP synthesis in the absence of electrochemical H+ gradients.     

Cellular UDP-glucose deficiency caused by a single point mutation in the UDP-glucose pyrophosphorylase gene

We previously isolated a mutant cell that is the only mammalian cell reported to have a persistently low level of UDP-glucose. In this work we obtained a spontaneous revertant whose UDP-glucose level lies between those found in the wild type and the mutant cell. The activity of UDP-glucose pyrophosphorylase (UDPG:PP), the enzyme that catalyzes the formation of UDP-glucose, was in the mutant 4% and in the revertant 56% of the activity found in the wild type cell. Sequence analysis of UDPG: PP cDNAs from the mutant cell showed one missense mutation, which changes amino acid residue 115 from glycine to aspartic acid. The substituted glycine is located within the largest stretch of strictly conserved residues among eukaryotic UDPG:PPs. The analysis of the cDNAs from the revertant cell indicated the presence of an equimolar mixture of the wild type and the mutated mRNAs, suggesting that the mutation has reverted in only one of the alleles. In summary, we demonstrate that the G115D substitution in the Chinese hamster UDPG:PP dramatically impairs its enzymatic activity, thereby causing cellular UDP-glucose deficiency.     

Characterization of a lectin-like protein isolated from Lachesis muta snake venom

A lectin-like protein was isolated from L. muta venom by gel filtration on BIO Gel P-100 followed by column Chromatography on DEAE-sephades A-50. The protein eluted at 0.4 M Nacl in 0.01 Tris pH 7.3 and exhibited agglutinin activity toward 0+ human erythrocytes. The protein is a dimer with Mr 28 kDa. Amino acid analysis revealed high content of tryptophan and acid recidues and low content of cysteine and methionine residues. No neutral carbohydrates and sialic acid were detected. Circular dichroic spectrum shows 78% of B structure and 1% of alpha structure. In vitro experiments with erythrocytes from rat, rabbit and dog revealed strong agglutination while red blood cells from mice, sheep and goat were not agglutinated. In vivo experiments using anesthetized rats, a sharp and prolonged fall in the blood pressure was observed at protein dose of 1.5 mg/kg. Double dose of protein caused the death of the animal.