Human endothelin converting enzyme-2 (ECE2): characterization of mRNA species and chromosomal localization.

Generation of the functionally pleiotropic members of the endothelin vasoactive peptide family is critically catalyzed by unique type II metalloproteases, termed endothelin converting enzymes (ECE). Isolation of human ECE-2 (EC 3.4.24.71) cDNAs revealed deduced open reading frames of 787 and 765 amino acids with approximately 60% identity with human ECE-1. Characterization of mRNA variants revealed mRNA structural diversity at the 5'-terminus. Two mRNA species exist containing distinct first and second exons. Furthermore, in one of these species, an in-frame deletion of the intracytoplasmic domain removed 29 amino acids. Because of the previously reported human genetic diseases ascribed to germline mutations of member genes of the endothelin family, ECE2 was localized in human chromosomes with fluorescence in situ hybridization and radiation hybrid mapping to 3q28-q29 and SHGC-20171/D3S1571, respectively.     

Moramonas marocensis gen. nov., sp. nov.: a jakobid flagellate isolated from desert soil with a bacteria-like,but bloated mitochondrial genome

A new jakobid genus has been isolated from Moroccan desert soil. The cyst-forming protist Moramonas marocensis gen. nov., sp. nov. has two anteriorly inserted flagella of which one points to the posterior cell pole accompanying the ventral feeding groove and is equipped with a dorsal vane—a feature typical for the Jakobida. It further shows a flagellar root system consisting of singlet microtubular root, left root (R1), right root (R2) and typical fibres associated with R1 and R2. The affiliation of M. marocensis to the Jakobida was confirmed by molecular phylogenetic analyses of the SSU rRNA gene, five nuclear genes and 66 mitochondrial protein-coding genes. The mitochondrial genome has the high number of genes typical for jakobids, and bacterial features, such as the four-subunit RNA polymerase and Shine–Dalgarno sequences upstream of the coding regions of several genes. The M. marocensis mitochondrial genome encodes a similar number of genes as other jakobids, but is unique in its very large genome size (greater than 264 kbp), which is three to four times higher than that of any other jakobid species investigated yet. This increase seems to be due to a massive expansion in non-coding DNA, creating a bloated genome like those of plant mitochondria.     

中国生理学会八十周年回顾

The Chinese Association for Physiological Sciences (CAPS) celebrated her 80th anniversary last November. Eighty years ago, Dr. Robert K. S. Lim, Professor of Physiology at the Peking Union Medical College, in association with Dr. Wu Xian (Professor of Biochemistry) and Dr. B. E. Read (Professor of Pharmacology), sponsored the establishment of the Chinese Physiological Society.     

Studies on staphylococcal enterotoxin B. III. Purification with absorbents]

The biological and immunological activities of Staphylococcal enterotoxin B are stable in pH 2.0 approximately 11.0, and also resistant to proteolytic enzyme (trypsin, pepsin) digestion for 3 approximate 4 hours. Therefore, the toxin could be purified with trypsin digest and then absorbed on kaolin and Kieselgel, followed by eluting the different pH buffer solutions. Further purifications was chromatographied on CM-Sephadex column.     

Biochemical properties of a penicillinase from Escherichia coli carrying Rms 298.

We obtained two R plasmids, i.e., Rms195 and Rms298, from a clinical isolate, E. coli GN5503. Penicillin beta-lactamase (PCase) was extracted from ML1410 Rms195+ and Rms298+, and was purified by chromatography. Rms195 PCase was identical to the type I PCase mediated by R-TEM, RI and Rms212. The isoelectric point of Rms298 PCase was 5.9 and its molecular weight was 21,000 +/- 1,000. The substrate profile and physiochemical properties indicate that Rms298 PCase belongs to the type IV PCase mediated by Rms139 isolated from Pseudomonas aeruginosa.     

Isolation and characterization of a new picornavirus in Taiwan]

During the 1971 outbreaks of acute hemorrhagic conjunctivitis, 298 cases were admitted to the Veterans General Hospital and seven strains of new picornavirus were isolated in human epidermoid carcinoma cells. Two strains of the virus isolated have been further studied. Serological neutralization indicated that these isolates might represent a distinct picornavirus group. Biophysical and biological properties determined by this study indicated that the viruses had many characteristics in common with the echoviruses such as morphological appearance, lack of essential lipids, acid stability, density in cesium chloride, sedimentation rate, growth in the presence of 5-iodo-2-deoxyuridine 5-bromo-2-deoxyuridine and nonpathogenicity to suckling mice. However, they were differentiated into 2 strains on the basis of plaque size and neutralization kinetics.     

Effects of cholera toxin on cellular and paracellular sodium fluxes in rabbit ileum

The diarrhea observed in patients which cholera is known to be related to secretion of water and electrolytes into the intestinal lumen. However, the exact mechanisms involved in these secretory processes have remained unclear. Although it is clear that purified toxin acts on epithelial cell metabolism, its activity on Na⁺ transport across intestinal mucosa is equivocal: reported either to prevent net Na⁺ absorption or to cause net secretion of Na⁺ from serosa to mucosa. Since total transmural Na⁺ fluxes across “leaky” epithelia involve very significant movement via a paracellular shunt pathway, we studied the effects of cholera toxin on the cellular and paracellular pathways of Na⁺ movement. Unidirectional Na⁺ fluxes were examined as functions of applied potential in control tissues and in tissues from the same animal treated with purified cholera toxin. Treatment of rabbit ileum in vitro with toxin stimulated the cellular component of serosa-to-mucosa Na⁺ flux (from $\text{2.41 ± 0.49 μ}\text{equiv./h}$ per cm² under control conditions to $\text{4.71 ± 0.43 μ}\text{equiv./h}$ per cm² after treatment with toxin, $\text{P < 0.01}$). The effect of cholera toxin on Na⁺ movement through the cells from mucosa to serosa appeared to be insignificant. Finally, a marked decrease in the Na⁺ permeability ($\text{P < 0.01}$) and no detectable significant changes in transference number for Na⁺ of the paracellular shunt pathway were observed following treatment with cholera toxin. These results provide direct evidence for the hypothesis that purified cholera toxin stimulates active sodium secretion but has minimal effect on sodium absorption.