Peter Mair verzorgt dit jaar namens de vakgroep Politicologie de cursus Grote Mogendheden voor bestuurskundestudenten in hun basisdoctoraal. Eenieder die deze collegereeks volgt zal duidelijk zijn... Show morePeter Mair verzorgt dit jaar namens de vakgroep Politicologie de cursus Grote Mogendheden voor bestuurskundestudenten in hun basisdoctoraal. Eenieder die deze collegereeks volgt zal duidelijk zijn dat hij zich zeer betrokken voelt bij de toestand in Noord-Ierland .Mair is dan ook zelf van Ierse afkomst. Onder begeleiding van professor Daalder schreef hij het proefschrift 'Changing the Irish Party System'. Peter Mair geeft hier een eerste schets van de problemen. Show less
Kamp, M.; Silvestrini, M.C.; Brunori, M.; Beeumen, J.; Hali, F.C.; Canters, G.W. 1990
By differential screening of a cDNA library of two-week-old rice seedlings cDNA clones were obtained, corresponding to shoot-specific mRNAs. By sequence analysis two of these clones were found to... Show moreBy differential screening of a cDNA library of two-week-old rice seedlings cDNA clones were obtained, corresponding to shoot-specific mRNAs. By sequence analysis two of these clones were found to be rbcS cDNA clones. The mRNA corresponding to a third cDNA clone (COS5) displayed an expression pattern similar to the expression pattern of rbcS genes. The mRNA (800 bases) was light-inducible and encoded by a single-copy gene. The genomic clone (GOS5) was isolated and the intron/exon structure was determined by comparing the nucleotide sequences of the mRNA and the genomic clone. The gene contains two introns. Transcription start sites were determined by S1-nuclease mapping and primer extension. The start site obtained by both methods is located 87 bp upstream of the translation start site and 23 bp downstream of TATA box-like sequence. In the 5' non-coding region motifs can be found that are homologous to sequences in promoters that are light- or UV-inducible or confer leaf-specific expression. The open reading frame present in GOS5 codes for a protein (15 kDa) that contains a putative chloroplast transit peptide and does not show any significant homology to protein sequences in the NBRF protein database. Show less
The isolation and purification of cytochrome C550 from the methylamine-oxidizing electron-transport chain in Thiobacillus versutus is reported. The cytochrome is a single-heme-containing type I... Show moreThe isolation and purification of cytochrome C550 from the methylamine-oxidizing electron-transport chain in Thiobacillus versutus is reported. The cytochrome is a single-heme-containing type I cytochrome c with a relative molecular mass of 16 +/- 1 kDa, an isoelectric point of 4.6 +/- 0.1, a midpoint potential of 272 +/- 3 mV at pH < 4 and 255 +/- 5 mV at pH = 7.0, and an axial coordination of the Fe by a methionine and a histidine. The midpoint potential decreases with increasing pH due to the deprotonation of a group tentatively identified as a propionate (pK(a) = 6.5 +/- 0.1 and 6.7 +/- 0.1 in the oxidized and reduced protein, respectively) and a change in the Fe coordination at pH > 10. The electron-self-exchange rate appears to depend strongly on the ionic strength of the solution and is relatively insensitive to changes in pH. At 313 K and pH 5.2 the electron-exchange rate amounts to 0.7 x 10(2) M-1 S-1 and 5.3 x 10(2) M-1 S-1 at I = 40mM and I = 200 mM, respectively. Amino acid composition and molar absorption coefficients at various wavelengths are reported. Resonances of heme protons and the epsilon-H3 group of the ligand methionine of the Fe have been identified in the H-1-NMR spectrum of the reduced as well as the oxidized cytochrome. Show less
Kamp, M. van de; Hali, F.C.; Rosato, N.; Finazzi Agro, A.; Canters, G.W. 1990
