CD is a common comorbidity in youth with type 1 diabetes. Differences in CD prevalence may reflect international variation in screening and diagnostic practices, and/or CD risk. Although glycemic control was not different, the lower height SDS supports close monitoring of growth and nutrition in this population.

The production by an organism of organic substances inimical to the life processes of other organisms and inhibiting their growth is known as antibiosis. The phenomenon of antibiosis has attracted wide-spread attention in recent years chiefly because of the remarkable chemotherapeutic effects of penicillin, a product of the mold Penicillium. The anabolic products of many kinds of bacteria,' molds,2 and algae,3 and substances elaborated by certain species of flowering plants4 can be readily demonstrated to have antibiotic properties when small amounts of the active materials are tested on microorganisms with suitable assay procedures. In view of the reported antibacterial activity of the green alga Chlorekla and the many antagonistic substances now known to be produced by numerous kinds of fungi, the lichens seemed to offer favorable material for antibiotic investigations, inasmuch as the bodies of these plants are comprised of mixtures of algae and fungi. Accordingly we have tested a considerable number of lichens for antagonistic action against some common species of bacteria, and offer herewith a preliminary report concerning some of our observations.Methods.-The lichens were brought in fresh condition to the laboratory, placed in shallow pans, and moistened with water for the purpose of allowing them to become physiologically more active. After a few hours of exposure to sunlight, samples of the moist lichens were separated from the substrata with a razor blade and forceps. Extracts were made by grinding, with a glass mortar and pestle, 100 mg. of lichen in 1 ml. of phosphate buffer solution adjusted to pH 7.4. The final aqueous extract was approximately pH 7.0. Extractions were carried out at room temperature and the samples were stored at 1°C. for a short time until the materials could be assayed. No attempt was made to clarify the extracts in these preliminary tests. The aqueous suspensions were assayed against Staphylococcus aureus, Escherichia co/i, Bacillus subtilis or other bacteria by means 250 PROC. N. A. S.

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COOH (peptide 204), targeted to the common C-terminus of human adenovirus 12 (Adl2) tumor antigens encoded by the ElA 13S mRNA and 12S mRNA, has been synthesized. Antibody prepared in rabbits against peptide 204 immunoprecipitated two proteins of apparent Mr 47,000 and 45,000 from extracts of [35S]methionine-labeled Adl2-early infected KB cells and a 47,000 protein from extracts of the Adl2-transformed hamster cell line, HE C19. Immunoprecipitation analysis of infected and transformed cells labeled with 32P, showed that both major Adl2 EIA T antigens are phosphoproteins. Immunofluorescence microscopy of Adl2-early infected KB cells with antipeptide antibody showed the site of ElA protein concentration to be predominantly nuclear. ElA proteins were detected by imtnunofluorescence at 4 to 6 h postinfection and continued to increase until at least 18 h postinfection. Antipeptide 204 antibody was used to analyze the proteins synthesized in Escherichia coli cells transformed by plasmids containing cDNA copies of the Adl2 EIA 13S mRNA or 12S mRNA under the control of the tac promoter (D.

The 31 human adenoviruses (Ad) form five groups (A-E) whose DNAs are <20% homologous by molecular hybridization. Ad5 (group C) DNA contains a 55,000-dalton protein probably covalently bound to each 5' terminus. This covalently bound protein may be analogous to polypeptides found in other viral and nonviral systems that are covalently bound to genomic DNAs or RNAs and that are thought to function in DNA or RNA replication. Because of the importance of proteins linked to nucleic acids, we have investigated whether DNAs from all five groups of human adenoviruses have terminal proteins, as well as the peptide relationships among the different terminal proteins. We show here that DNAs from Adl2, 7,2, 19, and 4, representing Ad groups A-E, respectively, all contain covalently bound proteins of about 55,000 daltons. To investigate the peptide relatedness among the terminal proteins, we prepared microgram quantities of covalently'bound protein from Ads in groups A-E and compared their chymotryptic and tryptic '251-labeled peptide maps. We, fiPAW that the covalently bound protein maps of the fi'e Ad groups 4e highly related and possibly identical. On the other hand, the tryptic and chymotryptic peptide maps of the major virion protein II and the core proteins V and VII of groupsB, C, and E Ads show considerable heterology. Assuming that the covalently bound protein is virally coded, the conserved primary sequence of these proteins suggests a major functional role for the protein in Ad replication. Because the genetic origin of the Ad covalently bound proteins is not established, our data are also consistent with the possibility that the protein is coded by a cellular gene.Proteins that are firmly associated with genomic DNAs or RNAs have recently been identified in viral and nonviral systems, including adenoviruses (Ad) (1-7), picornaviruses (8-10), small Bacillus bacteriophages (11-13), possibly papovaviruses (14, 15), ColEl and CoIE2 plasmids (16), replicating OX174 (17), and possibly Escherichia coli DNA (18,19). The linkage between these nucleic acids and proteins is very likely covalent and, in some cases, this has been formally proved. Covalently bound proteins (CBPs) are of great interest because they are widely believed to function in DNA or RNA replication. In the Bacillus bacteriophage and picornavirus systems, these proteins appear to be a viral gene product involved in viral genome replication. How these proteins function is not known, and studies on this point should be important to the overall understanding of nucleic acid replication.Ads provide an excellent model to study the replication of linear duplex DNA molecules in eukaryotic cells (reviewed in refs. [20][21][22]. Ad DNA replicates in an overall 5'-3' direction by a strand displacement mechanism, with initiation and termination occurring at or near both termini. At least three viral coded early proteins and almost certainly a variety of cell-coded proteins are involved in Ad DNA replication.There are at least 31 human Ad serotypes that fall...