Uteroglobin and related biochemical changes in the reproductive tract during early pregnancy in the rabbit

The macromolecular secretion products of the rabbit uterus are described. The biochemical and biological properties of uteroglobin are considered, and its synthesis and secretion in various endocrinological conditions are described. The release of uteroglobin from the endometrial epithelium is stimulated by progestagens such as progesterone and its synthetic analogues, although its synthesis has not yet been shown to be entirely dependent on progesterone. The biological function of uteroglobin is obscure. Several approaches to this long-standing probelm are discussed, including the passage of uteroglobin into the blastocyst. It is suggested that interference with the passage of uterine components into the blastocyst may inhibit implantation and provide a means of contraception.     

Reduction electrochimique des cetones insaturees—VII. Influence de l'acidite du milieu sur le comportement cathodique des cetosulfones

The ketosulfones are known to be reduced electrochemically, in weakly acidic medium with scission of the CS bond. Nevertheless, in strongly acidic media, the electroactive entity being the protonated form of the carbonyl group, the reaction may lead to pinacols. In the case of γ-ketosulfones, the electroreduction in very weakly protic media is followed by the loss of proton of the acidic substrate due to the effect of electrogenerated bases. This chemical cleavage of the CS bond yields to α-ethylenic ketones reducible at the electrolysis potentiel. On the other hand, for the long chained ketosulfones the reduction may occur through a partial intramolecular electron transfer.     

A prospective evaluation of Bass, Bionator and Twin Block appliances. Part I--The hard tissues

A prospective clinical study with a random allocation of 47 adolescent patients to three different functional appliance groups was established and compared with an untreated control group over a 9-month period. Treatment was undertaken with either a Bionator, Twin Block, or Bass appliance. Pre- and post-treatment cephalograms were used to quantify the skeletal and dentoalveolar changes produced by the appliances and compared with those observed in the control group as a result of growth. Both the Bionator and Twin Block appliances demonstrated a statistically significant increase in mandibular length (3.9 +/- 2.7 mm; 3.7 +/- 2.1 mm, respectively) compared with the control group (P < 0.05), with an anterior movement of pogonion and point B. Highly statistically significant increases (P < 0.01) were seen in lower face heights for all the appliance groups compared with the control group. The Twin Block group showed the least forward movement of point A due to a change in the inclination of the maxillary plane. The Bionator and Twin Block groups showed statistically significant reductions in the inclination of the upper incisors to the maxillary plane (P < 0.05). The Bass group showed minimal change in the inclination of the lower labial segment to the mandibular plane. The Bionator group demonstrated the greatest proclination of the lower labial segment (4.0 +/- 3.6 degrees). Clinically important changes were measured in all the appliance groups when compared with the control group. Differences were also identified between the functional appliance groups. The Twin Block appliance and, to a lesser extent, the Bionator appeared the most effective in producing sagittal and vertical changes.     

In vitro folding of Escherichia coli outer-membrane phospholipase A

Recombinant outer-membrane phospholipase A (OMPLA) of Escherichia coli was expressed without its signal sequence from the T7 phi 10 promoter. As a result of the cloning strategy the protein had an N-terminal extension of six amino acid residues. The protein accumulated in the cytosol in inclusion bodies. Conditions were established for the efficient folding of OMPLA in vitro in the presence of Triton X-100. After in vitro folding, the protein was present as a mixture of folded and unfolded forms. Ion-exchange chromatography was used for the purification of OMPLA and the separation of correctly folded, enzymically active enzyme from unfolded inactive protein. The final protein preparation was pure and fully heat-modifiable based on SDS/PAGE. The recombinant enzyme had a specific activity of 71 U/mg, which is similar to the value of the wild-type enzyme, purified from the membrane. The final yield of active enzyme was 35 mg protein/l culture of an A600 of 6. Circular dichroism spectroscopy revealed a high content of beta strand, in good agreement with a predicted beta-barrel structure of this outer-membrane protein.     

A low rate of reinfection following effective therapy against Helicobacter pylori in a developing nation (China)

Ascorbate peroxidase (APX) is a hydrogen peroxide-scavenging peroxidase which uses ascorbate (AsA) as the specific electron donor. APX has not been isolated in mammals. Ocular tissue contains AsA at high concentrations, and we detected APX activity in bovine retinal pigment epithelium (RPE) and choroid. We purified APX from bovine RPE and choroid by four chromatographic steps. The purified APX was a monomeric hemoprotein with a molecular mass of 43 kDa. The amino acid sequence of the amino-terminal region of the purified APX showed a high degree of homology to that of plants. The primary product of the APX reaction was identified as the monodehydroascorbate radical. The APX showed high specificity for AsA as an electron donor. This is the first isolation and characterization of APX from mammals, and its role in the protection against active species of oxygen in ocular tissue is discussed.     

Application of capillary electrophoresis in clinical chemistry--developments from preliminary trials to routine analysis

Since instruments performing capillary electrophoresis (CE) became commercially available in the late 1980s, information on this relatively new analytical technique has been increasing almost exponentially. At the beginning of the last decade, fundamental discoveries in the field were made mainly in the laboratories of analytical chemists; but now, this separation science is giving increasing impact to the laboratories of clinical chemists. This paper briefly reviews the history, instrumentation, different modes and theory of CE, and the prominent fields of its applications in clinical chemistry.     

The motor unit potential distribution over the skin surface and its use in estimating the motor unit location

Dextransucrase (DSRS) from Leuconostoc mesenteroides NRRL B-512F is a glucosyltransferase that catalyzes the synthesis of soluble dextran from sucrose or oligosaccharides when acceptor molecules, like maltose, are present. The L. mesenteroides NRRL B-512F dextransucrase-encoding gene (dsrS) was amplified by the polymerase chain reaction and cloned in an overexpression plasmid. The characteristics of DSRS were found to be similar to the characteristics of the extracellular dextransucrase produced by L. mesenteroides NRRL B-512F. The enzyme also exhibited a high homology with other glucosyltransferases. In order to identify critical amino acid residues, the DSRS sequence was aligned with glucosyltransferase sequences and four amino acid residues were selected for site-directed mutagenesis experiments: aspartic acid 511, aspartic acid 513, aspartic acid 551 and histidine 661. Asp-511, Asp-513 and Asp-551 were independently replaced with asparagine and His-661 with arginine. Mutation at Asp-511 and Asp-551 completely suppressed dextran and oligosaccharide synthesis activities, showing that at least two carboxyl groups (Asp-511 and Asp-551) are essential for the catalysis process. However, glucan-binding properties were retained, showing that DSRS has a two-domain structure like other glucosyltransferases. Mutations at Asp-513 and His-661 resulted in greatly reduced dextransucrase activity. According to amino acid sequence alignments of glucosyltransferases, alpha-amylases or cyclodextrin glucanotransferases, His-661 may have a hydrogen-bonding function.