Untersuchungen über die Wirkung des Cyanamids im Kalkstickstoff auf pathogene und nichtpathogene Mikroorganismen des Bodens

Ohne Zusammenfassung     

Dehalogenation of 4-chlorobenzoate by 4-chlorobenzoate dehalogenase from pseudomonas sp. CBS3: an ATP/coenzyme A dependent reaction

Pseudomonas sp. CBS3 was grown with 4-chlorobenzoate as sole source of carbon and energy. Freshly prepared cell-free extracts converted 4-chlorobenzoate to 4-hydroxybenzoate. After storage for 16 hours at 25 degrees C only about 50% of the initial activity was left. Treatment at 55 degrees C for 10 minutes, dialysis or desalting of the extracts by gel filtration caused a total loss of the activity of the 4-chlorobenzoate dehalogenase. The activity could be restored by the addition of ATP, coenzyme A and Mg2+. If one of these cofactors was missing, no dehalogenating activity was detectable. The amount of 4-hydroxybenzoate formed was proportional to the amount of ATP available in the test system whereas CoA served as a real coenzyme. A novel ATP/coenzyme A dependent reaction mechanism for the dehalogenation of 4-chlorobenzoate by 4-chlorobenzoate dehalogenase from Pseudomonas sp. CBS3 is proposed.     

Antioxidant effect of diethyldithiocarbamate on microsomal lipid peroxidation assessed by low-level chemiluminescence and alkane production

Different thiol-containing compounds, such as diethyldithiocarbamate (DDC), glutathione, penicillamine, and dithioerythritol have been chosen to study their effect on ascorbate/Fe-ADP-induced lipid peroxidation, detected by low-level chemiluminescence and alkane production. In the concentration range used, these thiols exerted a temporary protection against lipid peroxidation by lengthening the induction period; after overcoming this induction period, no substantial inhibition of either chemiluminescence or alkane production was observed. DDC was effective in protecting against lipid peroxidation in the nanomolar range, whereas the group of other thiol-containing molecules operated in the millimolar range.     

The ACTH-immunoreactive system in the brain of the white-crowned sparrow, Zonotrichia leucophrys gambelii (Passeriformes, Emberizidae)

The ACTH-immunoreactive (ir) system of the avian brain is particularly conspicuous in the male white-crowned sparrow (Zonotrichia leucophrys gambelii). The irperikaryal population is concentrated mainly within the tuberal region, projecting primarily in a dorsal direction: (i) into the striatum; (ii) into rostral diencephalic, septal, hyperstriatal, and thalamic areas; and (iii) into dorsal and ventral areas of the brain stem. Ir-fibers seemingly contact local non-immunoreactive neurons mainly in the accumbens nucleus, septum, dorsal thalamic nuclei, infundibular and interpeduncular nuclei, and in the rostral diencephalon. Neurohemal zones are not supplied by ACTH-ir terminals. Immunocytochemical problems arising from the complexity of the proopiomelanocortin molecule and its derived peptide components are discussed in relation to phylogenetically directed studies, and contradictory results.     

Studien an einer farbig beringten Population des Braunkehlchens (Saxicola rubetra)

Ohne ZusammenfassungMrs. Margaret M. Nice gewidmet zum 70. Geburtstag am 6. Dezember 1953In verkürzter Form vorgetragen vonK. Schmidt auf der 67. Tagung der D. O.-G. am 16. August 1953 in Köln. — 291. Ringfundmitteilung der Vogelwarte Radolfzell.     

Enzymatic amidation of recombinant (Leu27) growth hormone releasing hormone-Gly45

By chemoenzymatic synthesis the gene for a (Leu27) analogue of human growth hormone releasing hormone-Gly45 [(Leu27)GHRH-Gly45] was constructed, cloned and expressed in Escherichia coli as a fusion protein with beta-galactosidase under the control of the lac promoter and operator. Upon induction with isopropyl-D-thio-beta-galactopyranoside the fusion protein accumulated to a yield of 15-20% of the total cellular protein. After cyanogen bromide cleavage of the fusion protein the precursor peptide (Leu27)hGHRH-Gly45 was separated by extraction and purified by ion exchange and h.p.l.c.-RP18 chromatography. The purified peptide was analysed by sequencing, isoelectric focusing, amino acid analysis and amino acid analysis after V8 protease digestion. The carboxy-terminal glycine was subsequently amidated by PAM (peptidylglycine-alpha-amidating-monooxygenase), an enzyme which was isolated and characterized from fresh bovine pituitaries. Correct amidation of the penultimate amino acid, leucine, was verified by peptide sequencing with an authentic leucine amide reference.