Cell-associated hemagglutinin of classical Vibrio cholerae O1 with reference to intestinal adhesion

Abstract Extraction of Streptococcus mutans with the detergents HECAMEG and lauroyl sarcosinate preferentially extracted antigen D, previously identified as a low molecular mass wall-associated protein. Western blotting with specific antisera was used to demonstrate that this antigen is the HPr component of the sugar-phosphotransferase transport system. Non-denaturing electrophoresis indicated that HECAMEG selectively extracted only one of the two forms of HPr. It is suggested that this form of HPr may have a specific cell surface location.     

Dysbindin-1, a Schizophrenia-Related Protein,Functionally Interacts with the DNA- Dependent Protein Kinase Complex in an Isoform-Dependent Manner

DTNBP1 has been recognized as a schizophrenia susceptible gene, and its protein product, dysbindin-1, is down-regulated in the brains of schizophrenic patients. However, little is known about the physiological role of dysbindin-1 in the central nervous system. We hypothesized that disruption of dysbindin-1 with unidentified proteins could contribute to pathogenesis and the symptoms of schizophrenia. GST pull-down from human neuroblastoma lysates showed an association of dysbindin-1 with the DNA-dependent protein kinase (DNA-PK) complex. The DNA-PK complex interacts only with splice isoforms A and B, but not with C. We found that isoforms A and B localized in nucleus, where the kinase complex exist, whereas the isoform C was found exclusively in cytosol. Furthermore, results of phosphorylation assay suggest that the DNA-PK complex phosphorylated dysbindin-1 isoforms A and B in cells. These observations suggest that DNA-PK regulates the dysbindin-1 isoforms A and B by phosphorylation in nucleus. Isoform C does not contain exons from 1 to 6. Since schizophrenia-related single nucleotide polymorphisms (SNPs) occur in these introns between exon 1 and exon 6, we suggest that these SNPs might affect splicing of DTNBP1, which leads to impairment of the functional interaction between dysbindin-1 and DNA-PK in schizophrenic patients.     

The Structure of Detoxin D1

The structure of detoxin D₁, one of the main active principles of detoxio complex, has been established on the basis of the degradative studies and spectral evidences as depicted in formula (I).

Detoxin D₁ has been demonstrated to belong to a new class of the depsipeptide contained an amino acid designated detoxinine which was newly isolated as a natural product.     

Effects of winter flooding on phosphorus dynamics in rice fields

Limnology - Controlling phosphorous (P) loads from rice fields is important for the conservation of aquatic ecosystems, in part because P is relatively concentrated at its sources. Recently, winter...     

The Assignment of the 13C-NMR Spectrum of Lysocellin and Its Biosynthesis

The complete ¹⁸C-NMR assignment of lysocellin sodium salt has been obtained based on the ¹³C-¹³C double labeling method and comparison with its retroaldol degradation product as well as a structurally related polyether antibiotic, lasalocid A.

In parallel, the biosynthesis of lysocellin was investigated by feeding ¹³C-labeled precursors followed by analyzing the resulting labeling patterns of the ¹³C-NMR spectra; a pathway to the antibiotic molecule is suggested which proceeds through condensation of two butyrate, eight propionate and one acetate units.

In addition, a conversion of butyrate to propionate during the metabolic process has been disclosed.     

Ineffectiveness of Lipopolysaccharide for Preventing the Tolerance Induction in Bone Marrow-Derived Lymphoid Cells with Dinitrophenyl-Poly-l-(Glutamic Acid,Lysine)

The effect of endotoxin or lipopolysaccharide (LPS) on tolerance induction in bone marrow-derived lymphoid cells (B cells) was investigated. Dinitrophenylated amino acid copolymer-l-(glutamic acid, lysine) (DNP-GL) acts as a potent tolerogen on normal and DNP-primed B cells. LPS significantly enhanced the anti-sheep red blood cell plaque-forming cell (anti-SRBC PFC) response that occurred after the immunization with a low dose of SRBC. LPS did not induce the primary anti-DNP PFC response after the injection of DNP-GL, nor did it prevent the tolerance induction in normal and DNP-primed B cells that occurred after the administration of DNP-GL.