The Iseult whole-body MRI delivered its first images in October 2021. The masterpiece of this MRI is an actively shielded NbTi magnet providing a homogeneous magnetic field of 11.7 T within a 90 cm warm bore. A dedicated cryoplant was constructed to cool the magnet at 1.8 K using a superfluid helium bath and it is in nominal operation since March 2019. This paper will present the cryoplant design, as well as the connection of the cryogenic ancillary equipment with the magnet. Estimated thermal losses will be compared with experimental data collected since the beginning of the cooling phase. Then, we will describe the system maintenance and the periodic controls of the various pressurized components performed keeping the continuous nominal operation of the MRI. Finally, we will present the first lessons learned on this unique cryogenic system operation and possible options to improve its reliability.

A new innovative whole-body 11.7-T MRI magnet is currently being manufactured at Alstom Belfort as part the Iseult/Inumac project, a French-German initiative focused on very high magnetic field molecular imaging. It will be installed at the end of year 2016 in a neuroscience research center with other very high field MRI equipment, operating in France at CEA Saclay since November 2006. The main coil constructed from a stack of 170 double pancakes of 2-m diameter, with a finished height of 4 m and 50 t in weight, has been completed within required tolerances. The two shielding coils, vacuum impregnated solenoids of 4 m in diameter and 10 t in weight, have been also completed within tolerances. A crack has been discovered inside the 2-m diameter mandrel of the cryogenic correction coils. A new mandrel has been manufactured, with delivery in July 2015. The main coil and the shielding coils have been integrated inside the helium vessel, and the assembly of thermal shield and vacuum vessel is due to start, with completion expected by the middle of 2016. The magnet will be serviced by a separate cryogenic and electrical facility; the installation of this external equipment will be completed by the end of 2015 when the first phase of the commissioning will start. Full tests and commissioning of the magnet at 1.8 K are expected at NeuroSpin at the beginning of 2017.

The subject matter discussed in the paper is the prosodic properties of parenthetical expressions. In Chapter One, the findings of the current research on the prosody of parenthetical expressions in Polish are presented in comparison with an analysis of English and German. The author also briefly discusses the strengths and weaknesses of these solutions. Chapter Two includes a proposal for the description of the prosody of parenthetical expressions which takes into account their special function in the thematic-rhematic structure of the utterance. Linguistic material illustrating this concept was necessarily limited to chosen parenthetical expressions with adverbial participles.

A neuroscience research center with very high field magnet resonance imaging (MRI) equipment has been opened in November 2006 in the Neurospin site of French Atomic Energy and Alternative Energies Commission (CEA, Saclay, France). One of the imaging systems, the so-called Iseult project, will require a whole body 11.75 T MRI magnet with a 900-mm warm bore. The coil is made of a niobium-titanium conductor cooled by a He II bath at 1.8 K, permanently connected to a cryoplant. The main coil is made of a stack of 170 double pancakes submitted to a peak field up to 12 T. A demonstrator made of six reduced double pancakes using the conductor developed for this project has been designed, manufactured, and tested at CEA/Saclay. The objective was to demonstrate that the Iseult main coil winding pack is able to sustain the high stress level calculated, 170 MPa azimuthally and 110 MPa radially. This demonstrator has been successfully energized up to 6000 A in a background field. A maximum azimuthal stress of 225 MPa has been reached, much higher than the nominal Iseult value. This paper presents the design, the manufacturing, and the cryogenics test results of this demonstrator.

A neuroscience research center with a very high field magnetic resonance imaging (MRI) equipment was opened in November 2006 in the Neurospin site at CEA Saclay. One of the imaging systems requires a whole body 11.75 T MRI magnet with a 900 mm warm bore. Operating at a homogeneous field level of 11.75 T, the cryostat has external dimensions of 4.8 m in diameter and 5.0 m in length. With the large aperture and high field strength, this magnet represents a real challenge when compared to the largest MRI systems ever built. The coil is made from a copper-stabilized niobium-titanium conductor cooled by a superfluid helium bath at 1.8 K and permanently connected to a cryo-plant. The main coil is constructed from a stack of 170 double pancakes and the magnet is actively shielded by two large coils connected in series to fulfill the stray field specifications. The two shielding coils, each of about 4 m in diameter, are presently being manufactured by Alstom Power Systems STTG; Magnets, Belfort. This paper describes the design of these coils and presents the latest progress of their fabrication. Details are given of the winding technique, impregnation method, and the first results of electrical and geometrical tests.

The segment condensation of peptides on a solid phase (Aminosilochrom) in organic medium catalyzed by a subtilisin complex with sodium dodecylsulfate was studied. The dependence of the efficiency of the enzymatic coupling of tripeptides with the basic structure X-Ala-Ala-Y-OMe [where X = Z, Boc, or Dnp and Y = Leu or Glu(OMe)] on the spacer (Phe-Met-Gly-Gly) content on the support and on the structure of the acylating component was investigated. The tripeptide segments were successively coupled to Aminosilochrom containing the Met-Ala-Gly spacer, and the peptidylaminosilochroms Dnp-Ala-Ala-Leu-Ala-Ala-Leu-Ala-Ala-Glu(OMe)-Met-Ala-Gly- A and Dnp-Ala-Ala-Leu-Ala-Ala-Glu(OMe)-Ala-Ala-Leu-Met-Ala-Gly- A ( A is the Aminosilochrom residue) were obtained in satisfactory yields. It was shown by these examples that the second and third segments are attached in yields higher than that for the first segment and the coupling efficiency does not depend on the amino acid composition of the acylating component.

The subtilisin-sodium dodecyl sulfate complex was shown to catalyze the coupling of peptide segments on a solid phase in organic medium. By a two-stage enzymic condensation of peptide fragments on aminosilochrom ( A ) containing Met-Ala-Gly as a spacer, Dnp(or Boc)-Ala-Ala-Leu-Ala-Ala-Glu(OMe)-Met-Ala-Gly- A and Z-Ala-Ala-Glu(OMe)-Ala-Ala-Leu-Met-Ala-Gly- A were obtained. It was shown that the condensation products can be split off from the support using Met residue cleavage by BrCN.

The subtilisin-sodium dodecyl sulfate complex was shown to catalyze the coupling of peptide segments on a solid phase in organic medium. By a two-stage enzymic condensation of peptide fragments on aminosilochrom (A) containing Met-Ala-Gly as a spacer, Dnp(or Boc)-Ala-Ala-Leu-Ala-Ala-Glu(OMe)-Met-Ala-Gly-A and Z-Ala-Ala-Glu(OMe)-Ala-Ala-Leu-Met-Ala-Gly-A were obtained. It was shown that the condensation products can be split off from the support using the Met residue cleavage by BrCN.

It was shown that acetylated dipeptides, Ac-D-Phe-D-Phe-OH, Ac-L-Phe-L-Phe-OH, Ac-D-Phe-L-Phe-OH, and Ac-L-Phe-D-Phe-OH, are formed during D-phenylalanine racemization. The overall content of these dipeptides in the reaction mixture ranged from 40 to 60% depending on the reaction conditions. We concluded that, like alpha-aminoisobutyric acid, phenylalanine is prone to polymerization under racemization conditions.

The strain B-1166 differs from the other strains of Bacillus thuringiensis ssp. finitimus because it has two crystal types with different localization in the sporulating cell, i.e., inside and outside of exosporium membrane. Two dissociants of the strain were obtained containing only one of the crystal types. The initial strain produces at least three various delta-endotoxins (Fin2, Fin3, and Fin5) differing from all other known entomocidal proteins; Fin2 and Fin3 are similar to each other but differ from Fin5. Both crystal types contain the same endotoxins (Fin2, Fin3, and Fin5). In the B-1166 strain the site of crystal deposition is not determined by their protein composition.

Two ways for semi-enzymatic preparation of the peptide aldehydes are proposed: (1) enzymatic acylation of amino alcohols with acyl peptide esters and subsequent chemical oxidation of the resulting peptide alcohols with DMSO/acetic anhydride mixture or (2) enzymatic acylation of the preliminarily obtained by a chemical route amino aldehyde semicarbazones. Subtilisin 72, serine proteinase with a broad specificity, distributed over macroporous silica, was used as a catalyst in both cases. Due to the practical absence of water in the reaction mixtures the yields of the products in both enzymatic reactions were nearly quantitative. The second way seems to be more attractive because all chemical stages were carried out with amino acid derivatives, far less valuable compounds than peptide ones. A series of peptide aldehydes of general formula Z-Ala-Ala-Xaa-al (where Xaa-al=leucinal, phenylalaninal, alaninal, valinal) was obtained. The inhibition parameters for these compounds, in the hydrolysis reactions of corresponding chromogenic substrates for subtilisin and α-chymotrypsin, were determined.

Proteins of molecular weight 65 and 62 kD and having affinity for toxins Cry4B and Cry11A produced by Bacillus thuringiensis ssp. israelensis have been isolated from brush border membranes of Aedes aegypti larvae using affinity chromatography. Using a ligand blotting technique, we show that the binding of these proteins to the biotinylated toxins is reversible and that the two toxins compete for binding to the two proteins. These proteins are likely to be Cry4B and Cry11A toxin receptors in gut epithelial cells of Aedes aegypti larvae.

The glutamyl endopeptidase gene of Bacillus intermedius was cloned from a genomic library expressed in Bacillus subtilis and sequenced (EMBL accession number Y15136). The encoded preproenzyme contains 303 amino acid residues; the mature 23-kDa enzyme consists of 215 residues. The mature enzyme reveals 38% of identical residues when aligned with the glutamyl endopeptidase from Bacillus licheniformis, whereas only five invariant residues were found among all known glutamyl endopeptidases. The amino acid residues that form the catalytic triad (H47, D98, and S171) as well as H186 participating in the binding of the substrate carboxyl group were identified. It seems that the structural elements responsible for the function of glutamyl endopeptidases from various sources are highly variable.

A serine proteinase from roots of Taraxacum officinale Webb S. L. was isolated by affinity chromatography and gel-filtration on Superose 6R using FPLC. The enzyme is a 67-kD glycoprotein containing 54% carbohydrate which we have named taraxalisin. The substrate specificity of taraxalisin toward synthetic peptides and oxidized insulin B-chain is comparable with that of cucumisin from Cucumis melo and the subtilisin-like serine proteinase macluralisin from Maclura pomifera. The proteinase is inactivated by DFP and PMSF. Taraxalisin exhibits maximal activity at pH 8.0. The pH range for stability of the enzyme is narrow--6.0-9.0. The temperature optimum for the subtilisin-like activity is 40 degrees C. The N-terminal sequence of taraxalisin has 40% of its residues identical to those of subtilisin Carlsberg. Thus, the serine proteinase from dandelion roots is a member of the subtilisin family, which is evidently widespread in the plant kingdom.

The structural gene of the carboxypeptidase T (cpt) was successfully expressed in cell wall-less L-form cells of Proteus mirabilis. The DNA sequence encoding the PhoA leader peptide was fused with a truncated cpt gene encoding the mature enzyme. The modified gene in a pUC-based kanamycin resistance vector under the control of the lac promoter was transformed into L-form cells of P. mirabilis. They were able to produce the recombinant CpT both as a secretory and as a cell-bound insoluble form. The co-secretory processing of the PhoA leader peptide was quite efficient. The yield of the secreted CpT was not less than 20 mg l−1 and should be improvable.

A pair of highly degenerated primers was adapted to carry out a single-step PCR-detection of any known and probably unknown cry genes of classes cry1, cry4 and cry9 encoding for 130 kDa protein delta-endotoxins in the natural Bacillus thuringiensis (BT) strains. The Southern hybridization of the product has demonstrated that essentially remote cry-genes like cry1Aa and cry9A (cryIG) could be represented in the single amplificate if they are simultaneously present in the genome of the analyzed strain. Four genes were detected by the proposed scheme in the BT ssp. galleriae 11-67. One of them, gene cry1Ga1 was originally found and cloned using the PCR-amplification product obtained from the genomic DNA of this strain as a probe. The new gene was completely identical to one cloned by B. Lambert (unpublished, EMBL accession number Z22510) and essentially related to cryIM (EMBL accession number Y09326), renamed according to the new nomenclature as cry1Ga2.

The structural gene of the carboxypeptidase T (cpt) was successfully expressed in cell wall-less L-form cells of Proteus mirabilis. The DNA sequence encoding the PhoA leader peptide was fused with a truncated cpt gene encoding the mature enzyme. The modified gene in a pUC-based kanamycin resistance vector under the control of the lac promoter was transformed into L-form cells of P. mirabilis. They were able to produce the recombinant CpT both as a secretory and as a cell-bound insoluble form. The co-secretory processing of the PhoA leader peptide was quite efficient. The yield of the secreted CpT was not less than 20 mg l−1 and should be improvable.

P33 protein was isolated from the cell walls of Candida utilis. Homology between P33 and Bgl2p proteins from the cell walls of Saccharomyces cerevisiae was shown. The important role of these proteins in molecular organization of yeast cell walls was demonstrated using trypsin proteolysis and the "gene disruption" method.