FT-IR Spectroscopic Investigation of Hofmann Td-Type Complexes of 2-, and 3-Chloropyridine

Hofmann-type modified clathrate hosts containing 2- or 3-chloropyridine molecules attached to metal (II) tetracyanocadmate frame, with a given formula: M(Clpy)₂Cd(CN)₄ where M = Mn, Ni or Cd; Clpy = 2- or 3-chloropyridine, have been synthesised for the first time. Their FT-IR spectra are reported in the 400–4000 cm^-1 region. All the vibrational modes of coordinated Clpy are characterised. The spectral features of the compounds studied are found to be similar to each other indicating that they have analogous structures. The coordination effect on the Clpy modes is analyzed.     

Zur Synthese von Human-Big-Gastrin I

The synthesis of the tetratriacontapeptide amide corresponding to the revised primary structure of human big gastrin I is described. For this purpose the fragments were designed in view of the maximum use of those utilized in our previous synthesis of human big gastrin I according to the first sequence proposal. Consequently the key tripeptide-Pro-Pro-His- (sequence 7–9) was prepared in suitably protected form to be used as amino or carboxyl component for assembly of the segments 1–9 and 1–14, respectively. Final condensation of the latter nona- and tetradecapeptide derivatives with the C-terminal segments 10–34 and 15–34 via the azide and the dicyclohexylcarbodiimide/N-hydroxysuccinimide procedure, respectively, leads to crude fully protected human big gastrin I. Upon deprotection by exposure to trifluoroacetic acid in presence of ethanedithiol-(1,2) as scavanger, ion exchange chromatography and partition chromatography, the desired tetratriacontapeptide amide was isolated in satisfactory yield with a high degree of purity. The identical immunological behaviour of the synthetic material, if compared with that of natural human big gastrin I, represents ulterior strong evidence for the correctness of the newly proposed structure for this putative prohormonal form of the gastrins.

Kurzmitteilung:Wünsch E., Wendlberger G., Mladenova-Orlinova L., Göhring W., Jaeger E., Scharf R., Gregory R. A., Dockray G. J., Hoppe-Seyler's Z. Physiol. Chem.362, 179 (1981).     

When does the Haver property imply selective screenability?

We point out that in metric spaces Haver's property is not equivalent to the property introduced by Addis and Gresham. We prove that they are equal when the space has the Hurewicz property. We prove several results about the preservation of Haver's property in products. We show that if a separable metric space has the Haver property, and the nth power has the Hurewicz property, then the nth power has the Addis-Gresham property. R. Pol showed earlier that this is not the case when the Hurewicz property is replaced by the weaker Menger property. We introduce new classes of weakly infinite dimensional spaces.     

Selective screenability in topological groups

We examine the selective screenability property in topological groups. In the metrizable case we also give characterizations of Sc(Onbd,O) and Smirnov-Sc(Onbd,O) in terms of the Haver property and finitary Haver property respectively relative to left-invariant metrics. We prove theorems stating conditions under which Sc(Onbd,O) is preserved by products. Among metrizable groups we characterize the countable dimensional ones by a natural game.     

Topological groups and covering dimension

We consider a natural way of extending the Lebesgue covering dimension to various classes of infinite dimensional topological groups. The dimension function that we introduce extends Lebesgue covering dimension, has the hereditary property, and has a product theory that is more similar to the product theory for the finite dimensional case.     

On some questions about selective separability

CH implies that selective separability is not preserved by finite powers (solving [3, Problems 3.7 and 3.9]). In ZFC, selective separability does not imply H‐separability (solving [4, Problem 34]) (© 2009 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)     

Matrix metalloproteinase-7 facilitates immune access to the CNS in experimental autoimmune encephalomyelitis

Background  

Metalloproteinase inhibitors can protect mice against experimental autoimmune encephalomyelitis (EAE), an animal model for multiple sclerosis (MS). Matrix metalloproteinase-9 (MMP-9) has been implicated, but it is not clear if other MMPs are also involved, including matrilysin/MMP-7 – an enzyme capable of cleaving proteins that are essential for blood brain barrier integrity and immune suppression.