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Biomedical subjects

B C Wang

Publications and source records attributed to B C Wang.

At least 73 records · Page 4Linked to original sources
PubMed1994

A surface mutant (G82R) of a human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal.

A chimeric enzyme (GST121) of the human alpha-glutathione S-transferases GST1-1 and GST2-2, which has improved catalytic efficiency and thermostability from its wild-type parent proteins, has been crystallized in a space group that is isomorphous with that reported for crystals of GST1-1. However, a single-site (G82R) mutant of GST121, which exhibits a significant reduction both in vitro and in vivo in protein thermostability, forms crystals that are not isomorphous with GST1-1. The mutant protein crystallizes in space group P2(1)2(1)2(1), with cell dimensions a = 49.5, b = 92.9, c = 115.9 A, and one dimer per asymmetric unit. Preliminary crystallographic results show that a mutation of the surface residue Gly 82 from a neutral to a charged residue causes new salt bridges to be formed among the GST dimers, suggesting that the G82R mutant might aggregate more readily than does GST121 in solution, resulting in a change of its solution properties.

Amino Acid Sequence↗
PubMed1994

Antinociception without motor blockade after subarachnoid administration of S-(+)-ibuprofen in rats.

This study was designed to determine whether the nonsteroidal anti-inflammatory drug (NSAID) sodium S-(+)-ibuprofen (IB), can be used intrathecally as a substitute analgesic for opiates to avoid the side effects of intrathecal narcotics. One week or more after surgical implantation of subarachnoid catheters, four groups of Sprague-Dawley rats were given 0.05 ml subarachnoid injections containing one of the following: Group A, normal saline (NS); Group B, IB 0.25 mg, 0.5 mg and 1.5 mg; Group C, morphine (M) 0.05 mg and 0.025 mg; Group D received NS or IB 1.5 mg. Animals were sacrificed for spinal cord examination one week after injection. Tail flick response latency (TFL) was determined before and 15, 30, 60, 120 and 180 minutes after each injection. TFL differences were compared. IB 1.5 mg vs NS, IB 0.5 mg vs NS, IB 0.25 mg vs M 0.05 mg, IB 0.25 mg vs M 0.025 mg, M 0.05 mg vs NS, and M 0.025 vs NS showed p < 0.05. IB 1.5 mg vs M 0.05 mg and M 0.025 mg, IB 0.5 mg vs M 0.05 mg and M 0.025 mg revealed no significant difference. No motor impairment was observed in any animal. Light microscopy of the spinal cord revealed no evidence of pathological changes in any animal (group D).

Analysis of Variance↗
PubMed1993

Crystal structure of bacteriophage T7 RNA polymerase at 3.3 A resolution.

The crystal structure of T7 RNA polymerase reveals a molecule organized around a cleft that can accommodate a double-stranded DNA template. A portion (approximately 45%) of the molecule displays extensive structural homology to the polymerase domain of Klenow fragment and more limited homology to the human immunodeficiency virus HIV-1 reverse transcriptase. A comparison of the structures and sequences of these polymerases identifies structural elements that may be responsible for discriminating between ribonucleotide and deoxyribonucleotide substrates, and RNA and DNA templates. The relative locations of the catalytic site and a specific promoter recognition residue allow the orientation of the polymerase on the template to be defined.

Bacteriophage T7↗
PubMed1993

The shear strength and the failure mode of plasma-sprayed hydroxyapatite coating to bone: the effect of coating thickness.

Plasma-sprayed hydroxyapatite coated (HAC) 50 and 200 microns thick on Ti-6Al-4V cylinders was transcortically implanted in the femora of canines to evaluate in detail the effect of coating thickness on the pushout shear strength and failure mode examined under scanning electron microscope after the periods of 4, 6, 8, and 12 weeks. The HAC coating exhibited higher shear strength at 50 microns than at 200 microns. Its failure mode was conclusively at or near the HAC-bone interface, and the slight attack of body fluid had not degraded the implant to the extent that failure occurred at the HAC-Ti alloy interface after 12 weeks of observation. For 200 microns-HAC, failure was found at the HAC-bond interface, inside the HAC lamellar splat layer and at the HAC-Ti alloy substrate interface, depending on the period of implantation. It was also deduced that the variation of failure mode of 200 microns-HAC with time could not be accounted for by the attack of body fluid alone; the degradation must be a synergetic adverse result of residual stress in the HAC and the attack of body fluid.

Analysis of Variance↗
PubMed1993

Striatal glucose consumption in chorea-free subjects at risk of Huntington's disease.

Controversial data have been reported with regard to the diagnostic value of the positron emission tomographic (PET) measurement of striatal glucose consumption (rCMRGlc) in chorea-free subjects at risk of Huntington's disease (HD). For further clarification of this issue we measured striatal and cerebellar rCMRGlc in 27 chorea-free subjects at risk of HD, 20 patients with manifest HD and 20 control subjects, using PET and 18F-fluorodeoxyglucose. In 6 of the at-risk subjects cerebellar ratios of striatal rCMRGlc were decreased below the corresponding 99% confidence limit determined in the controls. This indicates that the PET measurement of rCMRGlc may, indeed, be valuable in establishing the diagnosis of incipient HD in presymptomatic at-risk subjects.

Adolescent↗
PubMed1992

Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors.

The three-dimensional structure of the Bowman-Birk type proteinase inhibitor (PI-II) has been determined by x-ray crystallography and refined at 2.5-A resolution. This protein is a specific inhibitor of trypsin. Two reactive site loops, one at each end of the PI-II molecule, are structurally similar to each other and to reactive-site loops of pancreatic secretory trypsin inhibitor (Bolognesi, M., Gatti, G., Menegatti, E., Guarneri, M., Marquart, M., Papamokos, E., and Huber, R. (1982) J. Mol. Biol. 162, 839-869) and bovine pancreatic trypsin inhibitor (Deisenhofer, J., and Steigemann, W. (1975) Acta Crystallogr. B31, 238-250). PI-II is the first reported Bowman-Birk type inhibitor structure to be refined at high resolution, providing further insight into inhibitor mechanisms.

Amino Acid Sequence↗
PubMed1992

Lumbar subarachnoid ethylenediaminetetraacetate induces hindlimb tetanic contractions in rats: prevention by CaCl2 pretreatment; observation of spinal nerve root degeneration.

Disodium ethylenediaminetetraacetate (Na2EDTA) has replaced sodium bisulfite as the antioxidant in 2-chloroprocaine, Nesacaine CE. This study was undertaken to determine whether this new formulation has neurotoxic effects when administered in the subarachnoid space. Sprague-Dawley rats receiving subarachnoid injections of 1.5 mM or higher concentrations of Na2EDTA immediately initiated a circling behavior that was followed by the development of tetanic contractions of the hindlimbs lasting for 15-20 min. The tetanic contractions were followed by a brief period of hindlimb paralysis. Pretreatment of rats by subarachnoid injections of 1 mM CaCl2 prevented the development of tetanic contractions and paralysis of the hindlimb. Histologic examination of animals receiving Na2EDTA revealed moderate to severe focal degenerative changes in spinal nerve roots. Control rats receiving subarachnoid injections of normal saline solution did not develop tetanic contraction nor pathological changes on light microscopy. These results suggest that the preservative used in Nesacaine-MPF may be neurotoxic.

Animals↗
PubMed1992

[Detection of hepatitis B virus DNA in leucocytes of primary hepatocarcinoma using polymerase chain reaction].

The detection of HBV DNA in sera and leucocytes of 30 primary hepatocarcinoma patients whom were negative for HBsAg by reverse passive hemagglutination using polymerase chain reaction (PCR) were reported. The detectable rates of HBV DNA in leucocytes and sera were 86.7% and 70% respectively and the serological indexes, 43.4%. These indicated that HBV DNA may existent in blood of the patients with negative serological indexes. It was common that HBV DNA presented in peripheral leucocytes of primary hepatocarcinoma, indicated that extrahepatic sites of the HBV genome, and perhaps replication of HBV virus, existed. It was of great importance for the role of HBV DNA in lemology and epidemiology, etiology of hepatocarcinoma, diagnosis and treatment of infection as well as standard of cure.

Adult↗
PubMed1992

An experimental study on biomechanical properties of hepatic tissue using a new measuring method.

Hepatic tissue is an important internal organ for life. In this paper, we combined the moire method (an optical method) and indentation technique to investigate biomechanical response of hepatic tissue. To examine this measuring technique, we first measured the biomechanical properties of the block of pig's hepatic tissue using this method. The experimental result indicated that the pig's hepatic tissue was obviously a viscoelastic material. We closely analyzed the change of curves for force relaxation, creep, and nonlinear deformation of the block of pig's liver. Meanwhile, we also compared the changes in the biomechanical parameters of normal and cirrhosis hepatic tissue of humans.

Animals↗
PubMed1991

The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix.

The structure of the octameric histone core of the nucleosome has been determined by x-ray crystallography to a resolution of 3.1 A. The histone octamer is a tripartite assembly in which a centrally located (H3-H4)2 tetramer is flanked by two H2A-H2B dimers. It has a complex outer surface; depending on the perspective, the structure appears as a wedge or as a flat disk. The disk represents the planar projection of a left-handed proteinaceous superhelix with approximately 28 A pitch. The diameter of the particle is 65 A and the length is 60 A at its maximum and approximately 10 A at its minimum extension; these dimensions are in agreement with those reported earlier by Klug et al. [Klug, A., Rhodes, D., Smith, J., Finch, J. T. & Thomas, J. O. (1980) Nature (London) 287, 509-516]. The folded histone chains are elongated rather than globular and are assembled in a characteristic "handshake" motif. The individual polypeptides share a common central structural element of the helix-loop-helix type, which we name the histone fold.

Animals↗
PubMed1991

Crystals of a bovine neurophysin II tripeptide complex.

A bovine neurophysin II S-methyl-Cys-Tyr-Phe-NH2 complex has been crystallized using ammonium sulfate as the precipitating agent. The crystals are orthorhombic, the space group is either I222 or I2(1)2(1)2(1) with a = 124.9 A, b = 69.6 A and c = 151.5 A. The crystals diffract to at least 3.0 A resolution. Based on one neurophysin tetramer per asymmetric unit, the Matthews coefficient is calculated to be 3.92 with a solvent content of 69%.

Amino Acid Sequence↗
PubMed1991

Refined crystal structure of Cd, Zn metallothionein at 2.0 A resolution.

The crystal structure of Cd5,Zn2-metallothionein from rat liver has been refined at 2.0 A resolution of a R-value of 0.176 for all observed data. The five Cd positions in the asymmetric unit of the crystal create a pseudo-centrosymmetric constellation about a crystallographic 2-fold axis. Consequently, the distribution of anomalous differences is almost ideally centrosymmetric. Therefore, the previously reported metal positions and the protein model derived therefrom are incorrect. Direct methods were applied to the protein amplitudes to locate the Cd positions. The new positions were used to calculate a new electron density map based on the Cd anomalous scattering and partial structure to model the metal clusters and the protein. Phases calculated from this model predict the positions of three sites in a (NH4)2WS4 derivative. Single isomorphous replacement phases calculated with these tungsten sites confirm the positions of the Cd sites from the new direct methods calculations. The refined metallothionein structure has a root-mean-square deviation of 0.016 A from ideality of bonds and normal stereochemistry of phi, phi and chi torsion angles. The metallothionein crystal structure is in agreement with the structures for the alpha and beta domains in solution derived by nuclear magnetic resonance methods. The overall chain folds and all metal to cysteine bonds are the same in the two structure determinations. The handedness of a short helix in the alpha-domain (residues 41 to 45) is the same in both structures. The crystal structure provides information concerning the metal cluster geometry and cysteine solvent accessibility and side-chain stereochemistry. Short cysteine peptide sequences repeated in the structure adopt restricted conformations which favor the formation of amide to sulfur hydrogen bonds. The crystal packing reveals intimate association of molecules about the diagonal 2-fold axes and trapped ions of crystallization (modeled as phosphate and sodium). Variation in the chemical and structural environments of the metal sites is in accord with data for metal exchange reactions in metallothioneins.

Amino Acid Sequence↗
PubMed1991

Crystals of isoenzyme 3-3 of rat liver glutathione S-transferase with and without inhibitor.

The isoenzyme 3-3 of rat liver glutathione S-transferase (GST 3-3) isolated from a baculovirus expression system has been crystallized with and without inhibitor. The crystals grown in the absence of an inhibitor belong to space group P2(1) with cell dimensions a = 119.7, b = 96.2, c = 136.7 A and beta = 103.3 degrees, and diffract to 3 A resolution. The crystals grown in the presence of an inhibitor belong to space group C2 with cell dimensions a = 88.3, b = 69.7, c = 81.4 A and beta = 105.3 degrees, and diffract to at least 2.5 A resolution. The inhibitor used is either methylmercury chloride or ethylmercury chloride; both are weak inhibitors.

Animals↗
PubMed1991

Crystallographic analysis of the neurophysin-oxytocin complex. A preliminary report.

Single crystals of a bovine neurophysin II-oxytocin complex have been obtained using (NH4)2SO4 as the precipitating agent. The crystals diffract to at least 2.7 A resolution, belong to Laue group 4/mmm and exhibit systematic absences consistent with either space group P4(1)2(1)2 or P4(3)2(1)2. The cell dimensions are a = b = 69.07 A and c = 113.26 A. The crystals contain one neurophysin-oxytocin dimer per asymmetric unit. Based on a Vm of 2.9 A3/Da, the solvent content is calculated to be 58%. Chromatographic analysis of the dissolved crystals suggests the presence of three oxytocin molecules per neurophysin dimer.

Animals↗
PubMed1991

Preliminary crystallographic analysis of cardiotoxin V with major fusion activity from Taiwan cobra (Naja naja atra) venom.

Crystals of a cardiotoxin from Taiwan cobra venom have been obtained by the vapor diffusion method using methyl pentanediol as precipitant. The crystals belong to the hexagonal space group P6(1)22 (or P6(5)22), with cell dimensions a = b = 47.5 A, c = 111.3 A, alpha = beta = 90 degrees and gamma = 120 degrees and diffract to a resolution of 2.2 A. There is one molecule per asymmetric unit and the solvent content is estimated to be 53%.

Cobra Cardiotoxin Proteins↗
PubMed1991

Crystal structure of a bovine neurophysin II dipeptide complex at 2.8 A determined from the single-wavelength anomalous scattering signal of an incorporated iodine atom.

The crystal structure of a dipeptide complex of bovine neurophysin II has been solved at 2.8 A resolution solely by using single-wavelength anomalous scattering data from a single iodinated derivative. The asymmetric unit is an elongated tetramer of dimensions 110 x 40 x 30 A, composed of two dimers related by pseudo twofold symmetry. Each monomer consists of two homologous layers, each with four antiparallel beta-strands. The two regions are connected by a helix followed by a long loop. Monomer-monomer contacts involve antiparallel beta-sheet interactions, which form a dimer with two layers of eight beta-strands. One peptide per monomer occupies the principal hormone-binding pocket formed by part of the amino-terminal region and parts of the connecting helix and loop, with binding to protein consistent with conclusions drawn from solution studies. Dimer-dimer contacts involve the Tyr49 region adjacent to this site. A fifth dipeptide, of unknown biological significance, helps to stabilize one of the monomer-monomer interfaces and the tetramer-tetramer network in the crystal.

Amino Acid Sequence↗