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•Carbapenemase-producing Enterobacteriaceae (CPE) osteomyelitis is a rare condition.•Treatment of CPE osteomyelitis is complex and mainly based on triple antimicrobial therapy.•CPE osteomyelitides are mostly associated with functional status disability.

Rectal bleeding in neonates is an alarming event which suggests a possible necrotizing enterocolitis (NEC) but is usually the only symptom of an unexplained colitis characterized endoscopically by ecchymotic mucosal lesions, the so‐called ‘ecchymotic colitis’ (EC). We studied histologically and bacteriologically 18 infants (mean age: 18 days) presenting with rectal bleeding by systematic rectosigmoidoscopy and intestinal biopsies. The 18 infants were hospitalized. Prematurity was found in seven cases and an underlying condition in 14 cases (respiratory distress: six cases; infection: six cases; surgery: two cases). Histology showed a mild to moderate inflammation (10/12) of the mucosa with a prevalence of polymorphonuclear cells (8/10), frequent focal haemorrhages (11/12) and foci of pneumatosis (4/12). Numerous bacteria were seen in the mucus layer focally forming large clusters. Cultures of intestinal biopsies yielded exclusively Enterobacteriaceae species: Escherichia coli (seven cases), Klebsiella spp.(seven cases), and Enterobacter cloacae (three cases); four cases were sterile. Our study demonstrates that neonatal bleeding is associated with endoscopic and histological ‘ecchymotic colitis’ lesions and with a peculiar microbial flora of EBC strains. EC and necrotizing enterocolitis share similar features raising the question of the link between the two syndromes.

NADPH-cytochrome c(P-450) reductases from horse placenta and rat liver were purified and their biological activities compared using cytochrome cas substrate. Rat liver reductase was purified to electrophoretic homogeneity in one Chromatographic step on 2',5'-ADP agarose, and had a relative mass of 85 000 Da as estimated by SDS-PAGE. Equine placental reductase was separated from cytochrome P-450 on aminohexyl-Sepharose 4B and further purified on 2',5-ADP agarose; this preparation exhibited two bands, one of 85 000 and one of 80 000 Da, on SDS-PAGE. The lower molecular weight form was assumed to be a proteolytic product of the higher molecular weight form. A high retention of activity was obtained in both preparations. Equine placenta and rat liver enzymes were found to exhibit very similar V maxand K m, suggesting that they are not species specific.

NADPH‐cytochrome c(P‐450) reductases from horse placenta and rat liver were purified and their biological activities compared using cytochrome cas substrate. Rat liver reductase was purified to electrophoretic homogeneity in one Chromatographic step on 2',5'‐ADP agarose, and had a relative mass of 85 000 Da as estimated by SDS‐PAGE. Equine placental reductase was separated from cytochrome P‐450 on aminohexyl‐Sepharose 4B and further purified on 2',5‐ADP agarose; this preparation exhibited two bands, one of 85 000 and one of 80 000 Da, on SDS‐PAGE. The lower molecular weight form was assumed to be a proteolytic product of the higher molecular weight form. A high retention of activity was obtained in both preparations. Equine placenta and rat liver enzymes were found to exhibit very similar Vmaxand Km, suggesting that they are not species specific.

In bovine milk, a glycosylated phosphoprotein, component PP3, is known for its remarkable emulsifying properties and its capability to inhibit lipolytic activities. The determination of its primary structure is not sufficient to explain these properties. Secondary structure predictions of component PP3 and of its homologous proteins were achieved using a combination of multiple predictive methods. Based on this study, the f 119–135 region of component PP3 was proposed to be likely to adopt an amphipathic helical conformation, which is a lipid-binding motif. The conformation of the synthetic peptide corresponding to the C-terminal f 119–135 part of bovine component PP3 was analyzed by circular dichroism experiments using various media. The circular dichroism data indicated that the peptide was able to form an amphipathic α-helix structure in trifluoroethanol as well as in the presence of sodium dodecyl sulfate or acidic and neutral lipids, but not in water. Moreover, the conformation of this peptide is solvent dependent because it was found to adopt a β-sheet structure for low concentrations of sodium dodecyl sulfate or a low molar ratio of acidic lipid to peptide. Tensiometric measurements showed that the amphipathic C-terminal region of component PP3 is highly tensioactive and, thus, must be responsible for the particular behavior of the protein in emulsions.

In the stallion testis, aromatase activity was localized in the microsomal fraction. Androgen aromatization occurred through the loss of 1 beta,2 beta hydrogen atoms and appeared to involve free sulfhydryl groups. A single enzyme system seemed to aromatize androgen and norandrogen at the same rate while having a much lower affinity for norandrogens.

Studies using biochemical and pharmacologic approaches in steroidogenic cells and subcellular fractions have shown that the peripheral-type benzodiazepine receptor (PBR) is an outer mitochondrial membrane protein involved in the regulation of cholesterol transport from the outer to the inner mitochondrial membrane, the rate-determining step in steroid biosynthesis. Recent studies using gene targeting, antisense RNA, gene expression, and mutagenesis technology have demonstrated the obligatory role of PBR in cholesterol transport. In addition, the development of in vivomodels and ontogeny studies have validated data obtained in in vitroexperiments, confirming the role of PBR in steroidogenesis and suggesting that the presence of PBR is an absolute prerequisite for adrenocortical function.