Direct Synthesis of G-2N

The synthesis of angularly fused quinone natural products has been achieved using a photoenolization reaction and a Diels-Alder reaction in the key carbon-carbon bond forming steps.     

Thermodynamics of G-3(D4) and G-6(D4) carbosilanecyclosiloxane dendrimers

Temperature dependences of the heat capacity of G-3(D₄) and G-6(D₄) carbosilanecyclosiloxane dendrimers are studied for the first time by precision adiabatic vacuum and differential scanning calorimetry in the range of 6 to 350–450 K. Physical transformations in the investigated temperature range are observed and their standard thermodynamic characteristics are determined and discussed. Standard thermodynamic functions for a mole unit are calculated from the experimental data: C _p ^○ (T), H ^○(T), ? H ^○(0), S ^○(T) ? S ^○(0), and G ^○(T) ? H ^○(0) in the range of T → 0 to (350–449) K and standard entropies of formation at 298.15 K. Low-temperature (T ≤ 50 K) heat capacity is analyzed using the Debye theory of heat capacity of solids and the multifractal model. The values of fractal dimensionality D are determined and some conclusions on the topology of the investigated structures are drawn. The corresponding thermodynamic properties of the investigated carbosilanecyclosiloxane dendrimers under study are compared.     

G—34型耐硫甲烷化催化剂的反应特性

报道了在钼系与氧化物系催化剂基础上开发的G-34型耐硫甲烷化催化剂的反应特性。它综合钼系和氧化物系二类催化剂的优点,获得了活性高、选择性好、对原料气中硫浓度不敏感,反应前可自然硫化,有良好稳定性的结果。此催化剂用于压力粗煤气提高热值较经济合理。可直接生产合格的城市煤气。     

Cellulase and xylanase production byAspergillus sp. G-393

Applied Biochemistry and Biotechnology - The production of cellulase and xylanase can be achieved byAspergillus sp. G-393 using agricultural wastes. Enzymes produced by the strain G-393 were stable...     

Trennung von Makroglobulinen und Myelom-Proteinen durch Gelfiltration an Sephadex G-200

Ohne Zusammenfassung     

Purification and general biochemical properties of thermostable pullulanase fromBacillus stearothermophilus G-82

Thermostable extracellular pullulanase, produced by Bacillus stearothermophilus G-82 was purified to homogeneity from supernatants of continuous culture by ultrafiltration, ammonium sulphate precipitation, chromatography on Sephadex G-100, and DEAE cellulose. A mol wt of 53,000 was determined by gel filtration and 56,000 by SDS-polyacrylamide gel electrophoresis (SDS-PAGE). The isoelectric point (pI) was 4.2. The pullulanase contained predominantly acidic amino acids. The enzyme was optimally active at a temperature of 60 degrees C and pH 7.0. It preserved 100% of its activity after 10 min treatment at 60 degrees C. The thermostability was considerably increased in the presence of pullulan. Ca2+ did not increase activity or thermostability. Enzyme activity was fully inhibited by N-bromosuccinimide and partially by phenylmethylsulfonyl fluoride. Bacillus stearothermophilus G-82 pullulanase was able to hydrolyze alpha 1-6 as well as alpha 1-4 glucosidic bonds in pullulan, amylopectin, amylose, glycogen, and dextrin. The enzyme showed highest affinity to pullulan (Km = 0.14).