Degradation of quinaldine by Alcaligenes sp. and by Arthrobacter sp.

AbstractTwo bacterial strains, which grew aerobically in mineral salt medium with quinaldine as sole carbon source, were isolated. These strains could be identified as Alcaligenes sp. and Arthrobacter sp. Alcaligenes sp. was adapted to higher concentrations of quinaldine in a continuous culture. Both strains accumulated one compound, identified as quinisatin, which decomposed chemically to anthranilic acid and isatin. Quinisatin spontaneously resulted from 3,4-dihydroxy-2-oxo-1,2-di-hydroquinoline

Therapeutic strategies to slow chronic kidney disease progression

Childhood chronic kidney disease commonly progresses toward end-stage renal failure, largely independent of the underlying disorder, once a critical impairment of renal function has occurred. Hypertension and proteinuria are the most important independent risk factors for renal disease progression. Therefore, current therapeutic strategies to prevent progression aim at controlling blood pressure and reducing urinary protein excretion. Renin-angiotensin-system (RAS) antagonists preserve kidney function not only by lowering blood pressure but also by their antiproteinuric, antifibrotic, and anti-inflammatory properties. Intensified blood pressure control, probably aiming for a target blood pressure below the 75th percentile, may exert additional renoprotective effects. Other factors contributing in a multifactorial manner to renal disease progression include dyslipidemia, anemia, and disorders of mineral metabolism. Measures to preserve renal function should therefore also comprise the maintenance of hemoglobin, serum lipid, and calcium-phosphorus ion product levels in the normal range

Cloning and high-level expression of a chloroperoxidase gene from Pseudomonas pyrrocinia in Escherichia coli

AbstractA chloroperoxidase gene from Pseudomonas pyrrocinia was cloned into Escherichia coli using the cosmid vector pJB8. The gene coding for the chloroperoxidase could be localized to a 1.5 kb fragment of DNA which was subcloned into the high-copy-number plasmid pUC18. In one subclone increased halogenating activity could be found which was 570-fold greater than in P. pyrrocinia. The halogenating enzyme was identified as the chloroperoxidase by SDS-polyacrylamide gel electrophoresis

Zum Wirkungsmechanismus von 1-Nitroso-3-nitro-1-methyl-guanidin bei der Mutationsauslösung. 1. Wirkung von 1-Nitroso-3-nitro-1-methyl-guanidin auf die Matrizenaktivität der Polynucleotide bei der zellfreien Proteinsynthese

The effect of NNMG on the template activities of different polynucleotides (polyuridylic acid, polycytidylic acid, polyadenylic acid and copolymer of adenylic and guanylic acid 5,5:1) and t-RNS was studied. The maximum inhibition of the messenger activity was found for poly-C, followed by poly-Α and poly-U. The acceptor activity of t-RNA was found to be inhibited by NNMG: maximum for proline, followed by serine, leucine, phenylalanine and lysine. The mechanism of these inhibitions was studied using NNMG radioactively labelled on the methyl group. Different amounts of radioactivity were found in the various polynucleotides and t-RNS