Inhibition of HIV-1 replication by a tricyclic coumarin GUT-70 in acutely and chronically infected cells

The anti-HIV-1 activity of GUT-70, a natural product derived from the stem bark of Chlophyllum brasiliense, was evaluated. GUT-70 inhibited HIV-1 replication in both acutely and chronically infected cells through suppression of NF-κB. Our results strengthen the idea that NF-κB pathway is one of the potential targets to control HIV-1 replication and that GUT-70 could serve as a lead compound to develop novel therapeutic agents against HIV-1 infection.     

Studies on the Proteolytic Enzymes of Black Aspergilli

In order to determine the specificity of Aspergillus Saitoi protease, the hydrolyzate of B-chain of insulin oxidized by this enzyme was investigated on paperchromatography according to the 2,4-dinitrofluorobenzene technique. Specificity was compared with pepsin and other proteolytic enzymes.     

Structure of Phrymarolin-II

From root extracts of Phryma leptostachya L. was isolated a new lignan. Its structure has been determined to be 1-acetoxy-2-(3,4-methylenedioxy)phenoxy-6-(2-methoxy-4,5-methylenedioxy)phenyl-3,7-dioxabicyclo[3.3.0]octane on the basis of the chemical properties and spectra of its degradation products.     

Synthesis of 4-Thiazolone Derivatives Related to Firefly Oxyluciferin

Several 4-thiazolone derivatives were synthesized by condensation of appropriate aryl cyanide and ethyl thioglycolate (or derivative), and factors affecting to the reaction rate are discussed. Keto-enol tautomerization of the 4-thiazolones is briefly discussed.     

Crystallization and Properties of N-Benzoylglycine Amidohydrolase from Pseudomonas putida

N-Benzoylgiycine amidohydrolase (hippurate hydrolase EC 3.5.1.32), which catalyzes the hydrolysis of hippuric acid to benzoic acid and glycine, was found in a cell-free extract of Pseudomonas putida C692-3 grown on a medium containing hippuric acid. The enzyme was purified from the extract by ammonium sulfate fractionation and column chromatographies on DEAE-cellulose, DEAE-Sephadex A-50, hydroxyapatite, and Sepharose CL-6B. The enzyme was finally crystallized. The crystalline enzyme was almost homogeneous on electrophoresis. The enzyme had a molecular weight of about 170,000 and consisted of four subunits identical in molecular weight (approximately 42,000). The enzyme hydrolyzed N-benzoylglycine most rapidly, and N-benzoyl-l-alanine and N-benzoyl-l-aminobutyric acid. The Km value for these substrates were 0.72 mm, 0.87 mm, and 0.87mm, respectively. The optimum pH of the enzyme reaction was 7.0 to 8.0 and the enzyme was stable from pH 6.0 to 8.0.     

Studies on the Proteolytic Enzymes of Black Aspergilli

The specificity of crystalline Asp. Saitoi proteinase on oxidized lysozyme has been investigated by application of the Sanger DNP-method.

It was found that this proteinase has a much broader specificity as compared with pepsin and Bac. subtilis proteinase.     

Solid State 13C-NMR Analysis of Cell Wall Components of Fusarium oxysporum

An abdominal fat accumulation complicated by high blood triglycerides is regarded as a risk factor of metabolic syndrome. Feeding powdered nacre, mother of pearl, from Pinctada maxima, resulted in reduced body weight, visceral fat amount, and blood triglyceride level without influencing the food intake, body length, or amount of muscular tissue, suggesting that nacre powder specifically could decrease visceral fat.