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Articles by Lin Pan
Total Records ( 2 ) for Lin Pan
  Ming-Qi Liu , Rong-Fa Guan , Xian-Jun Dai , Lan-Fang Bai and Lin Pan
  Polygalacturonases that hydrolyzed the α-(1,4) glycosidic linkages of pectin is one of widely used industrial enzymes and applied in food, feed, paper and pulp, fruit juice and textile industries. To improve the production of extracellular pectinase (PgA) by a newly isolated Aspergillus niger JL-15 strain, the conditions of solid-state fermentation (SSF) were optimized by response surface methodology (RSM). The maximum pectinase activity (525.70 IU g-1 dry fermentation product) was obtained at 12.10% orange peel powder, 3.20% ammonium sulfate employing wheat bran as the solid substrate, 51.10% moisture content and 75.00 h fermentation and was 4.10 times as high as that of the basic medium (125.80 IU g-1). SDS-PAGE analysis showed that the molecular mass of PgA was about 40.0 kDa. The PgA was optimally active at 45°C and pH 4.0 and was stable over a broader pH range (4.0-8.0). The Michaelis-Menten constant (Km) and maximal velocity (Vmax) of PgA for citrus pectin was 4.04 mg mL-1 and 40.16 μmol min-1 mL-1, respectively. The enzyme mediates a decrease in the viscosity of pectin associated with a release of small amounts of reducing sugar. High performance liquid chromatography (HPLC) analysis revealed that PgA liberated a series of oligogalacturonate from pectin with the digalacturonate (G2) and trigalacturonate (G3) as major products. The mode of action study showed that the enzyme was an endo-acting polygalacturonase.
  Scott D. Seiwert , Steven W. Andrews , Yutong Jiang , Vladimir Serebryany , Hua Tan , Karl Kossen , P. T. Ravi Rajagopalan , Shawn Misialek , Sarah K. Stevens , Antitsa Stoycheva , Jin Hong , Sharlene R. Lim , Xiaoli Qin , Robert Rieger , Kevin R. Condroski , Hailong Zhang , Mary Geck Do , Christine Lemieux , Gary P. Hingorani , Dylan P. Hartley , John A. Josey , Lin Pan , Leonid Beigelman and Lawrence M. Blatt
  Future treatments for chronic hepatitis C virus (HCV) infection are likely to include agents that target viral components directly. Here, the preclinical characteristics of ITMN-191, a peptidomimetic inhibitor of the NS3/4A protease of HCV, are described. ITMN-191 inhibited a reference genotype 1 NS3/4A protein in a time-dependent fashion, a hallmark of an inhibitor with a two-step binding mechanism and a low dissociation rate. Under preequilibrium conditions, 290 pM ITMN-191 half-maximally inhibited the reference NS3/4A protease, but a 35,000-fold-higher concentration did not appreciably inhibit a panel of 79 proteases, ion channels, transporters, and cell surface receptors. Subnanomolar biochemical potency was maintained against NS3/4A derived from HCV genotypes 4, 5, and 6, while single-digit nanomolar potency was observed against NS3/4A from genotypes 2b and 3a. Dilution of a preformed enzyme inhibitor complex indicated ITMN-191 remained bound to and inhibited NS3/4A for more than 5 h after its initial association. In cell-based potency assays, half-maximal reduction of genotype 1b HCV replicon RNA was afforded by 1.8 nM; 45 nM eliminated the HCV replicon from cells. Peginterferon alfa-2a displayed a significant degree of antiviral synergy with ITMN-191 and reduced the concentration of ITMN-191 required for HCV replicon elimination. A 30-mg/kg of body weight oral dose administered to rats or monkeys yielded liver concentrations 12 h after dosing that exceeded the ITMN-191 concentration required to eliminate replicon RNA from cells. These preclinical characteristics compare favorably to those of other inhibitors of NS3/4A in clinical development and therefore support the clinical investigation of ITMN-191 for the treatment of chronic hepatitis C.
 
 
 
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