Experimental investigation on moving chemical reaction boundary theory for weak-acid-strong-base system with background electrolyte KCl in large concentration.

In this report, the moving chemical reaction boundary (MCRB) was formed with the weak acid of acetic acid (HAc) and the strong alkali of NaOH, coupled with the excess of background electrolyte KCl. The experiments were compared with the predictions by the moving chemical reaction boundary equation (MCRBE). It is very interesting that (1) the experimental results are in good agreement with the predictions with the original MCRBE if the MCRB is an anodic moving boundary, (2) however, the experiments are extremely far away from the predictions with the original MCRBE if a cathodic moving boundary. Hence, the original MCRBE must be corrected under the later situation of cathodic moving MCRB. The corrected MCRBE was well quantitatively proved to be valid for the cathodic moving MNRB formed with the same electrolytes of HAc, NaOH and KCl.

Experimental study on moving neutralization reaction boundary created with the strong reactive electrolytes of HCl and NaOH in agarose gel.

In this paper, a moving neutralization reaction boundary (MNRB) is created with the strong reactive electrolytes of HCl and NaOH in agarose gel. The motions of the MNRB are investigated and compared with the predictions with the theory of the moving chemical reaction boundary (MCRB). The results show that, under appreciate experimental conditions, the experiments on the MNRB are exactly in coincidence with the predictions with the MCRB theory. Thus, the results excellently demonstrate that the MCRB theory is valid for the MNRB formed with the strong reactive electrolytes of HCl and NaOH. Additionally, it is, as discussed in this paper, imperative to develop a method to obtain ionic mobility at different temperatures and ionic strengths, in order to investigate the movements of the MCRB more efficiently.

Molecular analysis of the gene 6 from a porcine group C rotavirus that encodes the NS34 equivalent of group A rotaviruses.

The complete nucleotide sequence of the gene 6 from the porcine group (Gp) C rotavirus strain Cowden was determined from gene 6-specific clones selected from a cDNA library and from viral transcript RNA. The gene is 1348 nucleotides in length with a potential initiation codon beginning at nucleotide 25 and a stop codon at nucleotide 1231. The deduced protein contains 402 amino acids. Comparison of the gene 6 from this Gp C strain with sequences in the GenBank data base indicated that this gene shared homology with gene 7 of Gp A rotavirus strain SA-11 (22.9%) and gene 9 of Gp A rotavirus strain UK (22.6%), both of which encode the NS34 protein. In vitro translation products produced from transcripts generated from a gene 6 clone containing the entire open reading frame were not immunoprecipitated with either hyperimmune serum specific for the Gp C Cowden strain or a monoclonal antibody directed against the group antigen (VP6) of the Cowden strain. However, products generated from a full-length gene 5 clone of the Cowden strain were immunoprecipitated by each of these antibodies. These data suggest that in contrast to the Gp A viruses in which the gene 6 encodes the major inner capsid protein VP6, the gene 6 of the Cowden Gp C strain encodes a nonstructural protein corresponding to the NS34 of Gp A rotaviruses.

Sequence conservation of gene 8 between human and porcine group C rotaviruses and its relationship to the VP7 gene of group A rotaviruses.

cDNA libraries from porcine group (Gp) C rotavirus strain Cowden and a human Gp C rotavirus strain were generated. The complete nucleotide sequence of gene 8 from the Cowden strain was determined from gene 8-specific clones and viral transcript RNA. A full-length gene 8 clone was generated from the human Gp C virus by polymerase chain reaction (PCR) using primers deduced from the 3' and 5' ends of the Cowden strain gene 8, and the sequence of the human Gp C gene 8 was determined from this clone and gene 8 clones in the cDNA library. The gene 8 from the Cowden or the human Gp C strain is 1063 nucleotides in length and contains a long open reading frame beginning at the 49th nucleotide from the 5' end and terminating with a stop codon 16 bases from the 3' end. The encoded protein contains 332 amino acids (predicted molecular weight of 37.3 kDa) with two potential N-linked glycosylation sites in the porcine strain and three in the human strain. The polypeptide products derived from in vitro translation of the transcript RNA generated from a porcine gene 8 clone containing the entire open reading frame were analogous in size with the Gp A VP7. The gene 8 of porcine and human Gp C rotaviruses exhibited considerable nucleotide and deduced amino acid sequence identity (83.8 and 88.0%, respectively). Comparison of the Gp C gene 8 protein sequence with the VP7 protein of Gp A rotavirus revealed structural similarities, although the overall amino acid identity was low (less than 30%). These data suggest that the gene 8 of the porcine or human Gp C rotavirus encodes a protein corresponding to the VP7 outer capsid glycoprotein of Gp A rotaviruses and that the eighth gene is highly conserved in the porcine and human Gp C strains examined in this study.