Massive transformation and absolute stability

Under carefully chosen conditions, solidification theory may be applied to solid-state transformations, and this has been done here for composition-invariant diffusion transformations. The predictions of the modeling are compared with isovelocity experiments in two iron systems, Fe-7.29 wt pct Cr and Fe-3.1 wt pct Ni. The ferrite to austenite phase transformation is used to demonstrate that stabilization of a planar transformation front at absolute stability is the natural lower velocity limit for a composition-invariant (massive) transformation. The results of the model, which includes nonequilibrium effects, clearly show that steady-state plane-front growth leading to composition invariance can be obtained at various temperatures depending on the growth velocity. In the lower velocity range, at the limit of absolute stability (of the order of 10 μm/s in the systems studied), the transformation interface moves under conditions of local equilibrium, and the temperature corresponds to the lower solvus temperature. At higher velocity (of the order of the interface diffusion rate, which in these systems is of the order of cm/s), the transformation is predicted to proceed at temperatures close to T ₀. At even higher rates, atom attachment kinetic undercooling will decrease the transformation temperature with respect to T ₀. In some cases, this temperature might even drop below the lower solvus. This article is based on a presentation made at the symposium entitled “The Mechanisms of the Massive Transformation,” a part of the Fall 2000 TMS Meeting held October 16–19, 2000, in St. Louis, Missouri, under the auspices of the ASM Phase Transformations Committee.     

Zur Verantwortung des Informatikers-Militärische Anwendungen der Informatik

Ohne Zusammenfassung     

Bemerkungen zu “Himmelsbeobachtungen in karolingischer Zeit

Additional remarks are given for the data of auroras during the earlier centuries.     

Inhibition of Listeria monocytogenes on cold-smoked salmon by nisin and carbon dioxide atmosphere

The heat-stable enterotoxin of Escherichia coli binds to an intestinal receptor, guanylyl cyclase-C, and produces cGMP to induce diarrhea. Guanylin is an endogenous ligand of this receptor. In the present in vivo study, the intestinal water and ion secretion induced by mucosal application of 2 nmol/ml guanylin or 5 or 10 units/ml heat-stable enterotoxin into closed loops was compared in the rat. The characteristics of secretion induced by cAMP following intravenous perfusion of 1.2 nmol/100 g per h vasoactive intestinal peptide were compared to those induced by cGMP. Unidirectional Na+ and Cl- fluxes were estimated by addition of 22Na into the loop and i.v. injection of 36Cl. Guanylin induced less water and ion secretion than that produced by heat-stable enterotoxin in the colon, confirming the results of in vitro studies, and also in duodenum and ileum. The cAMP- or cGMP-mediated response had a similar pattern, i.e., an inhibition of Na+ absorption and an increase in anion secretion.     

Asthma mortality in New Jersey residents

We report an 11-year-old boy with active Epstein-Barr virus (EBV) infection who developed acute aphonia and had signs and symptoms of recurrent laryngeal nerve palsy. The association of isolated recurrent laryngeal nerve palsy and EBV infection has not previously been reported. This case report expands the spectrum of neurologic complications of EBV infection, and suggests that infectious mononucleosis should be considered in the differential diagnosis of acute aphonia in children.     

Continued fraction for formal laurent series and the lattice structure of sequences

Besides equidistribution properties and statistical independence the lattice profile, a generalized version of Marsaglia's lattice test, provides another quality measure for pseudorandom sequences over a (finite) field. It turned out that the lattice profile is closely related with the linear complexity profile. In this article we give a survey of several features of the linear complexity profile and the lattice profile, and we utilize relationships to completely describe the lattice profile of a sequence over a finite field in terms of the continued fraction expansion of its generating function. Finally we describe and construct sequences with a certain lattice profile, and introduce a further complexity measure.     

Chinongruppenhaltige Polymere als Träger zur Immobilisierung von Enzymen

Crosslinked poly(4-styrenesulfonic acid chloride) was reacted with 3-amino-4-hydroxyphenyl benzoate to give a reactive carrier after saponification and oxidation. Its binding ability was tested with α-chymotrypsin. The binding ability as well as the enzyme activity could be increased by introduction of spacers, e.g. ethylenediamine and hexamethylenediamine between the poly(styrene)-matrix and p-benzoquinone. Also crosslinked poly(vinyl alcohol) was reacted with p-benzoquinone to give a reactive carrier, which could also immobilize α-chymotrypsin. Some properties of the immobilized α-chymotrypsin as activity, pH-optimum and storage stability were investigated.     

The elusive role of the N-terminal extension of {beta}A3- and {beta}Al-crystallin

ß-Crystallins are structural lens proteins with aconserved two-domain structure and variable N- and C-terminalextensions. These extensions are assumed to be involved in quaternaryinteractions within the ß-crystallin oligomers orwith other lens proteins. Therefore, the production of ßA3-and ßAl-crystallin from the single ßA3/A1mRNA by dual translation initiation is of interest. These crystallinsare identical, except that ßAl has a much shorterN-terminal extension than ßA3. This rare mechanismhas been conserved for over 250 million years during the evolutionof the ßA3/A1 gene, suggesting that the generationof different N-terminal extensions confers a selective advantage.We therefore compared the stability and association behaviourof recombinant ßA3- and ßAl-crystallin.Both proteins are equally stable in urea- and pH-induced denaturationexperiments. Gel filtration and analytical ultracentrifugationestablished that ßA3 and ßA1 both form homodimers.In the water-soluble proteins of bovine lens, ßA3and ßA1 are present in the same molecular weight fractions,indicating that they oligomerize equally with other ß-crystallins.¹H-NMR spectroscopy showed that residues Met1 to Asn22 of theN-terminal extension of ßA3 have great flexibilityand are solvent exposed, excluding them from protein interactionsin the homodimer. These results indicate that the differentN-terminal extensions of ßA3 and ßA1 donot affect their homo- or heteromeric interactions.