Arthrobacter luteus

The approach of Casiot et al. [21] was soon accepted and followed in the held of Se speciation. Wrobel et al. [91] applied a bacterium (Arthrobacter luteus) derived lysing enzyme mixture added with PMSF to study the intermediary molecules of Se metabolism of Se-enriched yeast without proteolysis. In order to tailor the cell wall degrading mechanism to the samples under test, Michalke et al. [77] used bacterial lisozyme and pronase E, either alone or in combination, for the Se speciation of Se-enriched lactic acid bacteria. Independent and simultaneous experiments were carried out with the two enzymes, thus achieving outstanding total Se-extraction efficiency (85-105 percent) with the sole application of pronase E and relatively low chromatographic recovery (8-12 percent) (still... 

Another purified enzyme preparation which produces laminaripentaose from insoluble laminarin and from heat-treated pachyman is produced by a strain of Arthrobacter luteus (100,101,102) when grown on yeast cells or / -(1 —>3)-glucan. The enzyme, which was named Zymolase (also referred to as Zymolyase) appeared to be homogeneous by electrophoresis in a Tiselius apparatus and by ultracentrifugation. The molecular weight of the enzyme was estimated from ultracentrifugation to be ca. 20,500. The optimum pH for lysis of viable yeast cells was 7.5. The optimum temperature was 35°C. The optimum pH for heat-treated pachyman hydrolysis was 6.5, and the optimum temperature was 45°C. A Lineweaver-Burk plot with heat-treated pachyman yielded a Km value of 0.04% when the solubilized carbohydrate was assayed by the phenol-sulfuric acid method. Zymolase lost all its activity after incubation at 60°C for 5 min. 

Kaneko, Kitamura, and Yamamoto (99) studied the susceptibilities to lysis by crude enzyme from Arthrobacter luteus broth of 26 strains of yeast, representing 18 species and 8 genera, although most species belonged to Saccharomyces and Candida. Each yeast was tested during logarithmic and stationary phase of growth in different media. The... 

As well as clinical isolates, erm genes have been isolated from soil bacteria including antibiotic-producing microbes such as Bacillus licheniformis ermD [erm(D)]), B. sphaericus (ermG [erm(G) ), B. subtilis ermlM [erm C)]), B. anthracis (ermJ [erm(D)]), and B. licheniformis (ermK [erm(D)]) as well as Sac-charopolyspora erythreus (ermE erythromycin producer [erm E)]), Arthrobacter luteus (ermR or ermA, AR erythromycin producer [erm(R)]), and Streptomyces fradiae (ermSF [erm(S)]). 

Alu sequences in DNA were named for the enzyme Alu (obtained from Arthrobacter luteus), that which is able to cleave them. Alu sequences make up 6 to 8% of the human genome. In some cases of familial hypercholesterolemia, homologous recombination is believed to have occurred between two Alu repeats, resulting in a large deletion in the low- density lipoprotein (LDL) receptor gene. The LDL receptor mediates uptake of the cholesterol-containing LDL particle into many cell types and, in the absence of functional LDL receptors, blood cholesterol levels are elevated. Patients who are homozygous for this mutation may die from of cardiac disease as early as in their second or third decade of life. 

Arthrobacter luteus Bacillus amyloliquefaciens H Escherichia coll RY13 Haemophilus aegyptius Haemophilus influenzae Rj Moraxella species Microcoleus Nocardia otitidis Providencia stuartii 164 Serratia marcescens... 

A peptidoglycan, of different type from that of other species of Cellulo-monas, has been isolated from C. cartalyticum L-Lysine replaces ornithine and the interpeptide bridge consists of d-aspartyl-D-serine. The same peptido-glycan type has been identified in Arthrobacter luteus, Brevibacterium liticum, and Corynebacterium manihot. 

Studies on cyanobacterial monogalactosyl- and digalactosyldiacylglycer-ols are reported in particular from Phormidium tenue [104-106] and Fischer-ella ambigua [107]. Some of the products from P. tenue showed potent inhibitory activity towards tumor promotion (in in vitro assay of Epstein-Barr virus activation in Raji cells induced by 12-O-tetradecanoylphorbol-13-acetate). Additional novel structures with difference in carbohydrate backbone and fatty acid moieties have been published for glycoglycerolipids of Rhodobacter sphaeroides [108], Saccharopolyspora sp [109], Thermus aquaticus [110], the sponge-associated bacterium Micrococcus luteus [111], Arthrobacter atrocyaneus [112], and from the Mycobacterium avium-intra-cellulare complex [113]. 

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