La situation est mure en 2004 pour proposer un modele d’organisation pour les centres d’archives numeriques. Ce modele traduit, en termes de services et d’interfaces, de moyens et de competences humaines les fonctions et les concepts definis dans le modele de reference OAIS. Ce modele d’organisation structure l’Archive en trois services qui peuvent etre largement autonomes: la Collecte et la preparation des donnees, le Stockage d’archive, et enfin la Gestion des donnees et la communication. Les caracteristiques detaillees de ces trois services et les profils de competence necessaires a leur mise en œuvre seront analyses. Ce modele s’applique aux institutions patrimoniales dont la fonction premiere est de preserver les donnees dont elles ont la charge. Nous montrerons qu’il peut s’appliquer a d’autres types d’organismes et qu’il doit permettre la restauration de la fonction d’Archive au cœur du systeme d’information des entreprises et des administrations.

Le groupe de travail PIN (perennisation de l’information numerique) a ete cree en 2000 a l’occasion de la diffusion en France de la norme OAIS. Il regroupe des representants de grandes institutions publiques (CNES, BnF, CEA, etc.) et d’entreprises qui mettent en commun leurs reflexions et leurs experimentations concernant l’archivage de donnees scientifiques, patrimoniales ou operationnelles. PIN s’efforce de developper une culture commune aux differents acteurs de l’archivage.

Au départ, en 1995, il s'agit d'élaborer une norme dans le domaine de l'archivage des informations techniques et scientifiques produites et gérées par les agences spatiales.Or la question n'est pas spécifique au monde spatial ; elle a une portée beaucoup plus générale.Il est donc nécessaire d'intégrer dans la réflexion des représentants d'autres domaines professionnels concernés par l'archivage.C'est sur ces bases que le modèle de référence pour les systèmes ouverts d'archivage, dont nous donnons une description synthétique, a été conçu, valide aussi bien pour les archives d'entreprises que pour les organisations patrimoniales, applicable aussi bien pour les données scientifiques issues des expériences spatiales que pour les grandes bibliothèques.C'est une future norme internationale qui entame la dernière étape du processus de normalisation.ABSTRACT.It was, initially in 1995, a question of preparing a standard in the field of the archiving of technical and scientific information produced and managed by the Space Agencies.But the question was not specific to the space world and had a far more general scope.Representatives of other professional domains concerned by archiving had therefore to be integrated in the reflection.These were the bases used to design the Reference Model for an Open Archival Information System, of which a synthetic description is given, valid for corporate archives as for public heritage organizations, as applicable to scientific data from space experiments as to major libraries.This is now a future international standard about to undertake the last step of the standardization process.

The nonobese diabetic (NOD) mouse, in which major histocompatibility complex genes may be involved in the susceptibility to diabetes, has been developed as a model of autoimmune diabetes. The NOD mouse expresses I-A-encoded class II major histocompatibility complex antigens, which differ from those of other mouse haplotypes by the presence of a serine at position 57 of the A beta chain. Identifying islet autoantigens may help elucidate the role of class II antigens in the activation of autoreactive T cells and, thus, in the development of diabetes. We have detected autoantibodies directed against a 58-kDa islet cell antigen in NOD mice but not in other strains, including lupus-prone mice. Apart from insulin-secreting cells, the 58-kDa antigen was only found to be expressed by neuroblastoma cells and was identified as peripherin, an intermediate filament protein previously characterized in well-defined neuronal populations. This autoantigen cross-reacted with I-Anod class II antigens, suggesting that it may contribute to defective self-tolerance of islet beta cells in the NOD mouse.

Intermediate filament proteins of the rat insulinoma RIN5F cell line were characterized. Two-dimensional gel analysis followed by immunostaining of proteins demonstrated that these cells express both peripherin and the low-molecular-mass neurofilament protein (NF-L); this was confirmed for peripherin by immunohistochemistry, peptide analysis and Northern blot. No expression of these proteins could be detected with these same methods either in the adult pancreas or in the tumor at the origin of the cell line, although such expression was apparent on sections of rat pancreas at embryonal day 16. These results were compared to those obtained on the rat pheochromocytoma PC12 cell line: expression in the adrenal medulla of the embryo, no expression either in the adult tissue or in the tumor, but solely in the derived cell line. The expression of neuronal intermediate filament proteins in the rat insulinoma RIN5F cell line is discussed in relation to its similarity in the rat pheochromocytoma PC12 cell line, and its meaning as to the developmental cell lineage; an ectodermal origin is suggested for the pancreatic islet cells.

Peripherin, an intermediate filament protein, described recently, is expressed in well defined neuronal populations. We studied the phosphorylation, in vivo, of this protein in mouse neuroblastoma NIE 115 cell line and in sympathetic neurons labelled with [32P]-orthophosphate. The autoradiograms of proteins separated on two-dimensional polyacrylamide gels were compared with the Coomassie-blue stainings. The results show that peripherin occurs as a mixture of phosphorylated and non-phosphorylated isoforms, and that these forms coexist in both differentiated and non-differentiated cells. We demonstrate by cleavage at the unique tryptophan residue, a characteristic shared by most other intermediate filament proteins (IFP), that the phosphorylation sites are located on the amino-terminal half of peripherin as it is for vimentin and desmin. These results are discussed in relation to the organization of the filamentous network constituted by peripherin.

Three cDNA clones of 1.6 (3u), 1.2 (5g) and 0.6 (5b) kbp, specific for peripherin, a neuronal intermediate filament protein (IFP), have been isolated from a murine neuroblastoma cell lambda gt11 library by immunoscreening using peripherin antiserum. Antibodies eluted from the fusion proteins produced by clones 3u and 5g recognize the peripherin spots on immunoblots. Where they overlap the three cDNAs have identical sequences. cDNA 5g exhibits the closest homology to type III IFP cDNAs. cDNA 3u is identical to the corresponding region of cDNA 5g, except for the insertion of a 96 bp fragment at a position corresponding to the junction of exons 4 and 5 in type III IFP cDNAs. cDNA 5b is also identical to the corresponding region of cDNA 5g, except for the deletion of a 62 bp fragment at the junction of exons 8 and 9 in type III IFP cDNAs. S1 mapping experiments performed with probes covering the 3′ end of the two unexpected regions show that three distinct mRNAs correspond to the three cDNAs. Moreover, three peripherin products, two minor 61 and 56 kd products in addition to the major 58 kd peripherin, are observed when poly(A)+ RNA is in vitro translated, the 61 kd peripherin being translated from the 3u‐selected RNA. The three RNAs originate from alternative splicing of a unique peripherin gene, thus generating polymorphism of peripherin.

The mouse monoclonal antibody ME 101 raised against human peripherin, an intermediate filament protein (IFP) specific to well defined neuronal populations, recognizes all the major classes of vertebrate IFP in immunoblotting assays. Desmin, GFAP, vimentin, peripherin and the lightest neurofilament protein (NF-L) were cleaved into carboxy- and amino-terminal halves by N-chlorosuccinimide at their unique trytophan residue. Whereas the antibody directed against the epitope common to every IFP (intermediate filament antigen or IFA) and located on the carboxy-terminal end of the rod domain recognizes the carboxy-terminal half, the ME 101 antibody, as the present study illustrates, recognizes specifically the amino-terminal half. From the amino acid sequence data of IFP, it is deduced that the cognate epitope is localized on the amino-terminal part of coil la.

A 90-kDa protein-actin stable complex was purified from blood platelets by a short and efficient procedure giving at the same time actin used in polymerization assays. 90-kDa protein free of actin was prepared from the complex by 8 M ureau treatment and renaturation. By its molecular mass, immunological cross-reactivity with macrophage gelsolin and its effect on G- and F-actin the 90-kDa protein appears as the platelet gelsolin.

Human blood platelet actin was purified using 30% sucrose to extract actomyosin and potassium iodide to dissociate actomyosin and to depolymerize actin.Pure actin thus obtained resembles skeletic muscle actin in its polymerization properties, CD spectra and ability to activate myosin Mg2+‐ATPase.Isoelectric focusing gel analysis shows that human blood platelet actin exists in β and γ forms. The ratio of β to γ forms is of 5 in purified actin, in whole cell extract and in all the fractions studied.

FEBS LettersVolume 60, Issue 2 p. 414-418 Full-length articleFree Access Modification of the essential carboxyl group in octopine dehydrogenase C. Huc, C. Huc Laboratoire de Biochimie Cellulaire, Collège de France, Place Marcellin Berthelot, 75231 Paris Cedex 05, FranceSearch for more papers by this authorA. Olomucki, A. Olomucki Laboratoire de Biochimie Cellulaire, Collège de France, Place Marcellin Berthelot, 75231 Paris Cedex 05, FranceSearch for more papers by this authorF. Thomé-Beau, F. Thomé-Beau Laboratoire de Biochimie Cellulaire, Collège de France, Place Marcellin Berthelot, 75231 Paris Cedex 05, FranceSearch for more papers by this author C. Huc, C. Huc Laboratoire de Biochimie Cellulaire, Collège de France, Place Marcellin Berthelot, 75231 Paris Cedex 05, FranceSearch for more papers by this authorA. Olomucki, A. Olomucki Laboratoire de Biochimie Cellulaire, Collège de France, Place Marcellin Berthelot, 75231 Paris Cedex 05, FranceSearch for more papers by this authorF. Thomé-Beau, F. Thomé-Beau Laboratoire de Biochimie Cellulaire, Collège de France, Place Marcellin Berthelot, 75231 Paris Cedex 05, FranceSearch for more papers by this author First published: December 15, 1975 https://doi.org/10.1016/0014-5793(75)80761-7Citations: 14AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat References 1 N.V. Thoai, C. Huc, D.B. Pho, A. Olomucki, Biochim. Biophys. Acta, 191, (1969), 46– 57. 2 A. Olomucki, C. Huc, F. Lefébure, N.V. Thoai, Europ. J. Biochem., 26, (1972), 261– 268. 3 C. Huc, A. Olomucki, D.B. Pho, N.V. Thoai, Europ. J. Biochem., 21, (1971), 161– 169. 4 F. Thomé-Beau, A. Olomucki, Europ. J. Biochem., 39, (1973), 557– 562. 5 R.F. Colman, J. Biol. Chem., 248, (1973), 8137– 8143. 6 M.J. Adams, M. Buehner, K. Chandrasekhar, G.C. Ford, M.L. Hackert, A. Liljas, M.G. Rossmann, I.E. Smiley, W.S. Allison, J. Everse, N.O. Kaplan, S.S. Taylor, Proc. Nat. Acad. Sci. USA, 70, (1973), 1968– 1972. 7 D.B. Pho, A. Olomucki, C. Huc, N.V. Thoai, Biochim. Biophys. Acta, 206, (1970), 46– 53. 8 J.L. Bailey, Techniques in protein chemistry (1967), Elsevier Publishing Company Amsterdam 340– 352. 9 G. Ellman, Archiv. Biochem. Biophys., 82, (1959), 70– 77. 10 K.L. Carraway, D.E. Koshland Jr, Biochim. Biophys. Acta, 160, (1968), 272– 274. 11 A. Olomucki, F. Thomé-Beau, J.F. Biellmann, G. Branlant, Europ. J. Biochem., 56, (1975), 109– 116. 12 D.G. Hoare, D.E. Koshland Jr, J. Biol. Chem., 242, (1967), 2447– 2453. 13 F. Kurzer, K. Douraghi-Zadeh, Chem. Rev., 67, (1967), 107– 152. Citing Literature Volume60, Issue2December 15, 1975Pages 414-418 ReferencesRelatedInformation

The amino acid composition of octopine dehydrogenase from muscles of Pecten maximus was determined. The calculate dpartial specific volume of 0.74 allowed us to evaluate the molecular weight of the enzyme as 38000. It is concluded that this enzyme consists of a single polypeptide chain on the basis of the molecular weight determined from equilibrium ultracentrifugation in 6 M guanidine hydrochloride and from electrophoresis on polyacrylamide gel containing sodium dodecylsulfate as well as on the basis of the number of peptides obtained by tryptic digestion. The presence of one essential –SH group per mole of enzyme and of one binding site for NADH are also consistent with the existence of a single active center. No NH 2 ‐terminal amino acid can be detected by reaction with dansyl chloride and with phenyl‐isothiocyanate.