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Biomedical subjects

K S Hui

Publications and source records attributed to K S Hui.

At least 19 recordsLinked to original sources
PubMed2006

Potential use of a combined ozone and zeolite system for gaseous toluene elimination.

This study investigated the performance of a combined ozone and zeolite system in eliminating gaseous toluene which is a major contaminant in many industrial and indoor environments. The hypothesis that the removal of toluene by ozone can be substantially affected by confining the oxidation reaction in a zeolite structure was evaluated. The degradation of toluene seemed to be contributed by the active oxygen atom generated from the decomposition of ozone at the Lewis acid sites in the zeolite 13X. Air containing toluene levels at 1.5, 2 and 3 ppm was injected with ozone in the range of 0-6 ppm before being vented into a fixed amount of 3600 g zeolite 13X with 90 mm bed-length. The experimental results showed that the elimination rate of toluene was significantly enhanced when compared to using zeolite or ozone alone. In particular, over 90% of the 1.5 ppm toluene was removed when 6 ppm ozone was used at 40% relative humidity level. Deactivation of the zeolite 13X after a few hours of reactions under the current experimental conditions was probably due to the adsorbed water, carbon dioxide and the reaction by-products. The residue species left in the zeolite and the intermediate species in the exhaust gas stream were characterized by FT-IR, GC-MS and HP-LC methods, respectively. A distinctive peak of O atom attached to the Lewis acid site at 1380 cm(-1) was found in the FT-IR spectrum and trace amount of aldehydes was found to be the reaction by-products.

Air Pollutants↗
PubMed2006

Synthesis of MCM-41 from coal fly ash by a green approach: influence of synthesis pH.

The present study reports a green synthesis method for preparing pure (free of fly ash) and ordered MCM-41 materials from coal fly ash at room temperature (25 degrees C) during 24 h of reaction. It was shown that the impurities in the coal fly ash were not detrimental to the formation of MCM-41 at the tested conditions. The influence of initial synthesis pH on material properties of calcined MCM-41 samples was investigated by various techniques such as XRF, XPS, XRD, FTIR, DR-UV-vis, solid state NMR, N2 physisorption, TG-DTA, SEM and TEM. The experimental results showed that the amount of trace elements such as Al, Na, Ti and Fe incorporated into the sample increased with synthesis pH value. More aluminum species were incorporated with tetrahedral coordination in the framework under a high pH value. The particle size of the sample decreased with the synthesis pH value. Samples synthesized at high pH values had a larger pore size and were more hydrothermally stable than those at low pH values. From thermal analysis, it was observed that the synthesized MCM-41 samples showed a high thermal stability. These properties made the synthesized MCM-41 suitable for further processing into more useful materials in a wide range of applications.

Carbon↗
PubMed2006

Pure, single phase, high crystalline, chamfered-edge zeolite 4A synthesized from coal fly ash for use as a builder in detergents.

Single phase chamfered-edge zeolite 4A samples in pure form with a high crystallinity were synthesized by applying step-change of synthesis temperature during hydrothermal treatment of coal fly ash. The calcium binding capacity of these zeolite 4A samples (prepared from coal fly ash) and the commercial detergent grade zeolite 4A were tested for usage as a detergent builder. The results show that these zeolite 4A samples behaved similarly as the commercial one in removing calcium ions during the washing cycle. Moreover, from the leaching tests (evaluation of toxicological safety), the results show that these zeolite 4A samples leached the same elements (Sb, As, Se and Tl) as the commercial one with the concentrations in the same order of magnitude. This shows that the toxicological effect of the coal fly ash converted zeolite 4A was not worse than that of the commercial sample. Finally, economic and environmental aspects of converting coal fly ash to useful products were discussed.

Adsorption↗
PubMed2005

Removal of mixed heavy metal ions in wastewater by zeolite 4A and residual products from recycled coal fly ash.

The removal performance and the selectivity sequence of mixed metal ions (Co(2+), Cr(3+), Cu(2+), Zn(2+) and Ni(2+)) in aqueous solution were investigated by adsorption process on pure and chamfered-edge zeolite 4A prepared from coal fly ash (CFA), commercial grade zeolite 4A and the residual products recycled from CFA. The pure zeolite 4A (prepared from CFA) was synthesized under a novel temperature step-change method with reduced synthesis time. Batch method was employed to study the influential parameters such as initial metal ions concentration, adsorbent dose, contact time and initial pH of the solution on the adsorption process. The experimental data were well fitted by the pseudo-second-order kinetics model (for Co(2+), Cr(3+), Cu(2+) and Zn(2+) ions) and the pseudo-first-order kinetics model (for Ni(2+) ions). The equilibrium data were well fitted by the Langmuir model and showed the affinity order: Cu(2+) > Cr(3+) > Zn(2+) > Co(2+) > Ni(2+) (CFA prepared and commercial grade zeolite 4A). The adsorption process was found to be pH and concentration dependent. The sorption rate and sorption capacity of metal ions could be significantly improved by increasing pH value. The removal mechanism of metal ions was by adsorption and ion exchange processes. Compared to commercial grade zeolite 4A, the CFA prepared adsorbents could be alternative materials for the treatment of wastewater.

Adsorption↗
PubMed1998

A novel neuron-specific aminopeptidase in rat brain synaptosomes. Its identification, purification, and characterization.

A specific aminopeptidase localized exclusively in neurons of the central nervous system was identified with an automated continuous-flow aminopeptidase analyzer developed recently in this laboratory. The enzyme was purified from rat brain 4933-fold to homogeneity with 9.3% recovery by ammonium sulfate fractionation, followed by column chromatography successively on phenyl-Sepharose, Sephadex G-200, and twice on Mono Q FPLC. The purified single-chain enzyme was estimated to be 110 kDa in molecular mass. It has a pI of 5.25 and a pH optimum of 7.0. Only Mg(II) restores the activity of the apoenzyme. The neutral aminopeptidase hydrolyzes beta-naphthylamides of amino acids with aliphatic, polar uncharged, positively charged, or aromatic side chains. It has a Km of 95 microM and a kcat of 7.8 s-1 on methionine-enkephalin, releasing only the N-terminal tyrosine. The thiol-dependent metallo-enzyme is most sensitive to amastatin inhibition with a Ki of 0.04 microM, and is the aminopeptidase most sensitive to puromycin. Its properties are different from those of the ubiquitous puromycin-sensitive aminopeptidase obtained from the same enzyme preparation. The blocked N terminus, substrate and inhibitor specificity, hydrolytic coefficiency, metal effects, pI, molecular weight, and catalytic site show that this enzyme is distinct from all other known aminopeptidases. Its enrichment in the synaptosomes suggests that this first reported neuron-specific peptidase plays a role in neurotransmission and synaptic differentiation.

Amino Acid Sequence↗
PubMed1996

Differential expression of the soluble 170 kDa brain protein in the fetal and adult human brain.

The expression of the soluble 170 kDa brain protein (BP170) was studied in the developing human brain. Using immunohistochemical methods, it was possible to demonstrate that BP170 was expressed very strongly in the visual cortex up to approximately 27 weeks of gestation. After this time, the level of expression was reduced so that by adulthood the levels of BP170 were negligible. Similarly, BP170 was expressed in the hippocampus at all stages of development; however, unlike in the visual cortex, this protein was still apparent, albeit at low levels, in the adult. In addition, BP170 was co-expressed with tyrosine hydroxylase which suggests its possible role in the dopamine pathway.

Adult↗
PubMed1994

An endogenous aminoenkephalinase inhibitor: purification and characterization of Arg0-Met5-enkephalin from bovine striatum.

Arg0-Met5-enkephalin (Arg0-MEK) was isolated from bovine striatum and purified to homogeneity. The peptide was extracted with trichloroacetic acid, followed by column chromatography successively on Bio-Sil C8, semipreparative HPLC Radial-Pak C18, fast protein liquid chromatography (FPLC) Mono S, HPLC Ultrasphere-ODS, Supelco C18, Lichromsorb C18, and mu Bondapak C18. The peptide content was followed by radioimmunoassay with an antibody against synthetic Met-enkephalin. For each of the six HPLC and FPLC systems, the elution time of the immunoreactive fractions coincided exactly with that of synthetic Arg0-MEK. The purified peptide showed a highly homogeneous profile in three different analytical HPLC systems. Its retention time and three-dimensional UV spectrum were identical to those of the synthetic Arg0-MEK. The structure of the purified material was identified by microsequencing as the hexapeptide Arg-Tyr-Gly-Gly-Phe-Met. Ninety percent of the purified peptide was in oxidized form containing equimolar amounts of Met-(R)- and Met-(S)-sulfoxide. The reduced Arg0-MEK inhibited aminoenkephalinase with a Ki of 2.2 microM, and its sulfoxide analogue inhibited it with a Ki of 8.9 microM. The reduced or oxidized peptide suppressed the electrically induced contraction of rat vas deferens with an ED50 of 5 microM, and the effect could be reversed by equimolar naloxone. Our data indicate that Arg0-MEK is an immediate Met-enkephalin precursor and an endogenous inhibitor.

Amino Acid Sequence↗
PubMed1993

A new soluble brain-specific protein: identification and partial purification.

A new soluble 170-kDa protein (BP170) was found to be present exclusively in the brain of all the vertebrates that we studied by Western immunoblotting. It was not detected in peripheral rat tissues, including heart, kidney, liver, spleen, lung, muscle, adrenal, intestinal mucosa, sciatic nerve, or pituitary. In rat brain, its regional distribution was found to be heterogeneous, with its highest concentration in the cerebrum and its lowest in the hypothalamus, and 89% of it was in the post-microsomal fraction. BP170 constitutes at least 0.05% of the total brain cytosol proteins. Its level increases during development, being the lowest at 5 days and the highest at 90 days postnatal. BP170 is a single-chain polypeptide. It could be partially purified by precipitation with polyethylene glycol followed by column chromatography on Q Sepharose. Although BP170 was identified by an antiserum against puromycin-sensitive aminopeptidase (PSA), the two proteins differ in molecular weight, chromatographic properties, regional and subcellular distribution, developmental changes, immunoreactivity, and enzyme activity. Self-incubation or trypsin treatment of the partially purified BP170 generates no PSA activity, indicating that BP170 is not a PSA precursor. Furthermore, BP170 is neither an inhibitor nor an activator of PSA. Our data suggest that BP170 is a novel brain-specific protein not previously described.

Aminopeptidases↗
PubMed1993

Two cytosolic puromycin-sensitive aminopeptidase isozymes in chicken brain: molecular homology to brain-specific 14-3-3 protein.

Two puromycin-sensitive aminopeptidase isozymes (PSA-I and PSA-II) were isolated from chicken brain cytosol by ammonium sulfate fractionation followed by column chromatography on Cellex D and AH-Sepharose 4B and separated on Bio-Gel HTP. Each was purified to homogeneity on Sephadex G-200, Arg-Tyr-AH-Sepharose, Bio-Gel HTP, and preparative gel electrophoresis. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis, PSA-I appeared to be a monomer with a molecular mass of 105 kDa, and PSA-II to be composed of two subunits of 25 kDa and 100 kDa. The tryptic maps of 100 kDa and 105 kDa protein in HPLC are different in peak frequency, height, and composition. The internal peptide sequence of PSA-I has a considerable homology to PSA-II. Both isozymes have repeated copies of common peptide segments and have no significant sequence homology to other peptidases and proteinases. These thio and Co(2+)-activated isozymes have a neutral pH optimum and are inhibited by puromycin and bestatin. PSA-II is more sensitive to trypsin and heat treatment, has a lower Km to Met-enkephalin, and is more active on Arg BNA and Pro BNA. Our results suggest that PSA-I and PSA-II derive from translation of two RNAs of a new gene family related to the brain-specific 14-3-3 protein.

14-3-3 Proteins↗
PubMed1990

Cellular localization of puromycin-sensitive aminopeptidase isozymes.

We developed monoclonal antibodies (mAbs) against two isozymes of a cytosolic puromycin-sensitive aminopeptidase (PSA-I and PSA-II) purified from chicken brain. The isozymes could be distinguished using Ouchterlony double-immunodiffusion and Western immunoblot. Their distribution in neuronal and glial cells as visualized by indirect immunofluorescence with these mAbs was found to differ: PSA-I was confined mostly to glial lysosomes; PSA-II showed fibrillar distribution in both types of nerve cells, but in disparate patterns. These results and our findings of peptide structural differences suggest that the two PSA isozymes are expressed differently in the nervous system.

Aminopeptidases↗
PubMed1988

A novel dipeptidyl aminopeptidase in rat brain membranes. Its isolation, purification, and characterization.

A new type of dipeptidyl aminopeptidase, which releases basic aminoacyl dipeptides from the NH2-terminal end of oligopeptides, was purified about 2100-fold with 6.8% recovery from rat brain membranes by column chromatography on Cellex D, Arg-Tyr-AH-Sepharose 4B, hydroxylapatite, and Sephadex G-75, after the membranes were solubilized with Nonidet P-40. Activity was assayed by high performance liquid chromatography (HPLC) using Arg0-Met5-enkephalin (Arg0-enk)* as substrate in the presence of bestatin, thiorphan, and captopril. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the purified enzyme is apparently homogeneous with a mass of 64,000 daltons. This thiol enzyme is optimally active at pH 7 and is selectively activated by Mn(II). It loses 94% of its activity after EDTA treatment and can be reactivated by Mn(II), Co(II), and Zn(II). It splits Arg0-enk into equimolar amounts of Arg-Tyr and Gly-Gly-Phe-Met with a Km of 100 microM, and Vmax of 3.8 mumol/mg of protein/min. Dipeptidyl aminopeptidase does not hydrolyze model substrates for dipeptidyl aminopeptidases I, II, III, and IV, aminoacyl beta-naphthylamides, actin, desmin, tubulin, glial fibrillary acidic protein, and cytoskeletal neurofilament proteins. The enzyme is insensitive to puromycin, but is inhibited by several neuropeptides. Angiotensin III is the most potent with a Ki of 0.3 microM. Substrate specificity, pH optimum, molecular weight, activators, and catalytic site demonstrate that this enzyme is distinct from dipeptidyl aminopeptidases previously described.

Amino Acid Sequence↗
PubMed1988

Major rat brain membrane-associated and cytosolic enkephalin-degrading aminopeptidases: comparison studies.

The major cytosolic and membrane-associated enkephalin-degrading aminopeptidases were purified in parallel by column chromatography successively on DEAE-cellulose, AH-Sepharose, hydroxylapatite, Sephadex G-200, Affigel Blue, AH-Sepharose, and hydroxylapatite. With the final hydroxylapatite column, the cytosol (S) and the membrane (M) enzymes could each be resolved into two peaks, one eluted with 0.05 M phosphate (SI, MI) and the other with 0.25 M phosphate (SII, MII). The overall purification, with Arg BNA as substrate, for the SI and MI was about 450-fold; for SII and MII, 1,200-fold. The yield for each enzyme was about 2%. the major protein integral units of the four enzymes are similar; they are single polypeptide chains with a molecular weight of 100,000 daltons. Their pH optimum, substrate specificity, and sensitivity to puromycin show that they are similar to lysosomal aminopeptidase (EC 3.4.11.-). The two forms of the cytosol and the membrane enzymes have slightly different kinetic constants. With the inhibitors, SII is more sensitive to proctolin, whereas MII is more sensitive to bestatin and Arg-Phe-Ala. Mn2+ activates SI on Met-enkephalin degradation, but inhibits SII, MI, and MII.

Aminopeptidases↗
PubMed1988

Aminothiols: synthesis and effect on chicken brain aminopeptidases.

An amino acid derivative, leucinethiol, was reported to be a strong inhibitor of aminopeptidase activity. In order to obtain selective inhibitors of various brain aminopeptidases, we tested the inhibition by amino acid analogs of brain aminopeptidase activity. In particular, we synthesized the trifluoroacetyl derivatives of phenylalaninol, tyrosinol, and leucinol; leucinethiol; and phenylalaninethiol and measured their effect on soluble puromycin-sensitive aminopeptidase S1 and SII purified in our laboratory. Two of the compounds, L-bis (1-thio-2-amino-4-methylpentane) dihydrochloride (TAMP) and L-bis (1-thio-2-amino-3-phenylpropane) dihydrochloride (TAPP), caused significant inhibition.

Amphetamines↗
PubMed1988

Primary cardiac rhabdomyosarcoma: definition of a rare entity.

Primary cardiac rhabdomyosarcoma (PCR) is a highly malignant tumor that is rarely recognized prior to surgery or necropsy. We present the pathologic findings of a primary atrial rhabdomyosarcoma in an 82-year-old woman and an update on PCR as a clinicopathologic entity. In addition to pleomorphic tumor cells with cross-striations and a positive immunoperoxidase reaction for myoglobin, some areas of our patient's tumor had features of sarcoma botryoides. Electron optic studies showed primitive cells with fibroblastic and/or myoblastic differentiation. A comprehensive study of 77 cases in the international literature yielded new information and perspectives on PCR. The incidence of PCR is bimodal among males, being highest in infancy and early childhood with a secondary peak in the sixth and seventh decades. Females, however, have a single peak incidence in the fifth decade. Septal origin is 35.2% among infants and children but only 5.2% among adults. The predilection for the pediatric age group in conjunction with common septal origin among these patients suggests a congenital form of PCR that may arise from embryonic cell tests.

Aged↗
PubMed1987

The breakdown of the individual neurofilament proteins by cathepsin D.

In a continuing study of proteolysis of CNS proteins by CNS enzymes, neurofilament proteins (210 K, 155 K, 70 K) and desmin were separated, and the breakdown of individual proteins by purified brain cathepsin D was measured and compared to breakdown by plasma thrombin. With both cathepsin D and thrombin, the rate of breakdown of the 70 K protein was the highest, followed by the 155 K, and that of the 210 K was the lowest. With each substrate cathepsin D breakdown was the highest at pH 3; small but significant breakdown could be seen at pH 6. The pattern of intermediate breakdown products depended on pH, with greater amounts of fragments detected at higher pH, and the patterns with the two enzymes were different. We showed that differences exist in cleavage sites and breakdown rates of the neurofilament proteins. The capacity of the cathepsin D present in the tissue to hydrolyze these substrates was high, even at pH close to neutral, and was greatly in excess of that needed for physiological neurofilament turnover.

Animals↗
PubMed1987

Effect of several amino acid phosphonates and related compounds on rat brain aminopeptidases.

N-Terminal sodium phosphonate derivatives Na3O3PCH2CONHR (R-Leu, Phe, or Tyr) and Na3O3PCH2CONHR-R (R-R = Leu-Phe, Phe-Leu, Phe-Phe, and Phe-Tyr) were synthesized. All showed no activity toward a soluble rat brain aminopeptidase. We could not prepare the corresponding N-2-phosphono-2,2-diphenylacetyl compounds (Na3O3PC(C6H5)2CONHR) by the same Arbusov reaction. Little or no inhibition was obtained with the N-(2-hydroxy-2,2-diphenylacetyl derivatives HOC(C6H5)2CONHR (R = Leu, Phe, Trp, or Tyr). The best inhibitory responses were given by the N-(2-halogeno-2,2-diphenylacetyl mono- and dipeptides (Br/Cl)C(C6H5)2CONH Phe and (Br/Cl)C(C6H5)2CONHR-R (R-R = Leu,Leu, Leu-Phe, Phe-Gly, Phe-Leu, or Phe-Phe), respectively.

Amino Acids↗
PubMed1986

Separation and purification of individual neurofilament proteins by reverse-phase high-performance liquid chromatography.

A reverse-phase HPLC method was developed to separate individual neurofilament proteins (210,000, 160,000 and 70,000 Da) from the glial fibrillary acid protein. It is useful for analytical or preparative methods, with yields higher than 80%. The method represents improvement over previous methods in speed, efficiency, and purity. Combining this HPLC method with the conventional chromatographic method on DEAE-cellulose, highly purified individual neurofilament proteins can be obtained in large scale.

Animals↗