Kyungpook National University

About: Kyungpook National University is a education organization based out in Daegu, South Korea. It is known for research contribution in the topics: Population & Large Hadron Collider. The organization has 20497 authors who have published 42107 publications receiving 834608 citations.

Combination and QCD analysis of charm production cross section measurements in deep-inelastic ep scattering at HERA

Abstract: Measurements of open charm production cross sections in deep-inelastic ep scattering at HERA from the H1 and ZEUS Collaborations are combined. Reduced cross sections \(\sigma_{\rm red}^{c\bar{c}}\) for charm production are obtained in the kinematic range of photon virtuality 2.5≤Q2≤2000 GeV2 and Bjorken scaling variable 3⋅10−5≤x≤5⋅10−2. The combination method accounts for the correlations of the systematic uncertainties among the different data sets. The combined charm data together with the combined inclusive deep-inelastic scattering cross sections from HERA are used as input for a detailed NLO QCD analysis to study the influence of different heavy flavour schemes on the parton distribution functions. The optimal values of the charm mass as a parameter in these different schemes are obtained. The implications on the NLO predictions for W± and Z production cross sections at the LHC are investigated. Using the fixed flavour number scheme, the running mass of the charm quark is determined.

Biochemical properties and substrate specificities of alkaline and histidine acid phytases

Abstract: Phytases are a special class of phosphatase that catalyze the sequential hydrolysis of phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. Phytases are added to animal feedstuff to reduce phosphate pollution in the environment, since monogastric animals such as pigs, poultry, and fish are unable to metabolize phytate. Based on biochemical properties and amino acid sequence alignment, phytases can be categorized into two major classes, the histidine acid phytases and the alkaline phytases. The histidine acid phosphatase class shows broad substrate specificity and hydrolyzes metal-free phytate at the acidic pH range and produces myo-inositol monophosphate as the final product. In contrast, the alkaline phytase class exhibits strict substrate specificity for the calcium–phytate complex and produces myo-inositol trisphosphate as the final product. This review describes recent findings that present novel viewpoints concerning the molecular basis of phytase classification.