Oral-Fluid Thiol-Detection Test Identifies Underlying Active Periodontal Disease Not Detected by the Visual Awake Examination.

Periodontal disease in dogs is highly prevalent but can only be accurately diagnosed by performing an anesthetized oral examination with periodontal probing and dental radiography. In this study, 114 dogs had a visual awake examination of the oral cavity and were administered an oral-fluid thiol-detection test prior to undergoing a a full-mouth anesthetized oral examination and digital dental radiographs. The results show the visual awake examination underestimated the presence and severity of active periodontal disease.

Pilot evaluation of a novel test strip for the assessment of dissolved thiol levels, as an indicator of canine gingival health and periodontal status.

This study evaluated a novel test strip designed to assess thiol levels as they relate to gingival/periodontal health in dogs. The simple to use strip (similar in form to a pH test strip) provides a colorimetric signal which estimates the level of thiols dissolved in oral fluid. Among several oral sites tested (left and right lingual vestibules, lower buccal vestibule, and upper buccal gingival margin), fluid from the maxillary gingival margin gave results with the best dynamic range, and its thiol levels correlated well with several oral health parameters (Pearson coefficients between 0.

A simple saliva-based test for detecting antibodies to human immunodeficiency virus.

This study was performed to determine the feasibility of using saliva as a diagnostic medium for the detection of antibodies to human immunodeficiency virus type 1 (HIV-1) and HIV-2 under nonlaboratory conditions and to evaluate the performance characteristics of such a test. We developed for this purpose a self-contained kit (Saliva. Strip [ST]), which combines the collection and processing, as well as the analysis, of the specimen.

A simple whole-blood test for detecting antibodies to human immunodeficiency virus.

We developed an immunochromatographic whole-blood test (WBT) which detects antibodies to human immunodeficiency virus types 1 and 2 (HIV-1 and HIV-2) from fingerstick blood. The sensitivity and specificity of the WBT were 99.41% (1,018 confirmed positive patients) and 99.

A field test for the detection of antibodies to human immunodeficiency virus types 1 and 2 in serum or plasma.

In response to the need for simple and rapid tests for infectious diseases, we have devised a test for antibodies to human immunodeficiency virus type 1 (HIV-1) and HIV-2 which resembles many contemporary strip-style pregnancy tests in format and ease of use. The test was evaluated with 2,928 serum specimens (1,541 reactive and 1,387 nonreactive) collected and tested at a Mexico City hospital clinic and was compared with a laboratory assay (Abbott) performed simultaneously. The sensitivity and specificity of the test using these serum specimens were 99.

Simplified testing for antibodies to human immunodeficiency virus.

Test strips for the detection of antibodies to human immunodeficiency virus type 1 were investigated using specimens from risk groups in Thailand (141 reactive; 445 nonreactive) in a local Thai laboratory. The diagnostic sensitivity and specificity were both 100%. Using a set of seroconversion panels, the sensitivity of the test strips was within the range of sensitivities obtained with enzyme immunoassays.

Purification and properties of alternanase, a novel endo-alpha-1,3-alpha-1,6-D-glucanase.

A newly isolated soil bacterium strain NRRL B-21195, tentatively identified as a Bacillus species, was found to be a constitutive producer of a novel type of glycanase that hydrolyses in an endo-fashion the polysaccharide alternan, an alpha-1,3-alpha-1,6-D-glucan, referred to in the literature as B-1355 dextran (fraction S), synthesized from sucrose by alternansucrase of Leuconostoc mesenteroides. The glycanase, named alternanase, has been purified to homogeneity from a cell-free culture fluid of the bacillus grown in a liquid medium containing D-glucose, and has been characterized. The enzyme has a molecular mass of 110000 Da (SDS/PAGE) and an isoelectric point of approximately 4.

Two-dimensional gel analysis of serum apolipoprotein A-I isoforms: preliminary analysis suggests altered ratios in individuals with heart disease.

Apolipoprotein A-I (apo A-I), the major protein component of high-density lipoprotein, is quantified in a number of ways, typically by immunochemical methods. Commercial tests do not discriminate among isoforms of apo A-I. Two-dimensional electrophoresis, however, segregates and differentiates these isoforms, primarily due to charge variations among the various species.

High-molecular-weight amylase activities from bacteria degrading starch-plastic films.

Amylases having unusually high molecular weights (M(r), >150,000) were found in culture supernatants of an environmentally derived microbial mixed culture selected for its ability to utilize starch-containing plastic films as sole carbon sources. The mixed culture produced amylases active at pHs 5.5 and 8.

Computerized quantitative analysis of coomassie-blue-stained serum proteins separated by two-dimensional electrophoresis.

Two-dimensional electrophoresis in combination with Coomassie Blue staining was refined for use as a quantitative method. Microcomputer software was developed for use with the IBM AT and compatible computers for analyzing the gels. To test the refined method to determine its usefulness in simultaneous measurements of 28 human serum proteins, we measured each protein relative to a single standard (bovine serum albumin) polymerized at different concentrations in a calibration scale, rather than using 28 individual standards.

Biochemical characterization of a genetically altered calmodulin in Paramecium.

Recent evidence proposes that the calcium-binding protein, calmodulin, plays a crucial role in the regulation or modulation of the calcium-dependent potassium conductance in Paramecium tetraurelia (Hinrichsen, R.D., Burgess-Cassler, A.

A mutant Paramecium with a defective calcium-dependent potassium conductance has an altered calmodulin: a nonlethal selective alteration in calmodulin regulation.

The Paramecium mutant, pantophobiac A, has a defect that results in an in vivo loss of calcium-dependent potassium efflux channel activity. This defect is corrected fully by the microinjection of wild-type Paramecium calmodulin into pantophobiac A cells and is partially restored by calmodulins from other organisms, but it cannot be restored by microinjection of pantophobiac calmodulin. Overall, these results suggested that wild-type Paramecium calmodulin has unique features that allow it to restore fully a normal phenotype and that the defect in pantophobiac A might be an altered calmodulin molecule.

Restoration by calmodulin of a Ca2+-dependent K+ current missing in a mutant of Paramecium.

A combination of genetics, biochemistry, and biophysics was used to show that calmodulin is involved in the regulation of an ion channel. Calmodulin restored the Ca2+-dependent K+ current in pantophobiac, a mutant in Paramecium that lacks this current. The restoration of the current occurred within 2 hours after the injection of 1 picogram of wild-type calmodulin into the mutant.

Genetic analysis of mutants with a reduced Ca2+-dependent K+ current in Paramecium tetraurelia.

Two mutants of Paramecium tetraurelia with greatly reduced Ca2+-dependent K+ currents have been isolated and genetically analyzed. These mutants, designated pantophobiac, give much stronger behavioral responses to all stimuli than do wild-type cells. Under voltage clamp, the Ca2+-dependent K+ current is almost completely eliminated in these mutants, whereas the Ca2+ current is normal.

Permeabilization of Bacillus subtilis to chemotaxis methyltransferase II.

Treatment of Bacillus subtilis with 0.4% (vol/vol) toluene renders cells permeable not only to small molecules but also apparently to proteins as large as 30,000 daltons. Methyl-accepting chemotaxis proteins and two smaller polypeptides were methylated when B.

Functional homology of Bacillus subtilis methyltransferase II and Escherichia coli cheR protein.

A chemotaxis-related methyltransferase enzyme from Bacillus subtilis has been shown to methylate membrane-bound proteins in Escherichia coli in vitro. The methylated proteins are in the same molecular weight range as authentic E. coli methyl-accepting chemotaxis proteins.

Purification and characterization of Bacillus subtilis methyl-accepting chemotaxis protein methyltransferase II.

A Bacillus subtilis methyltransferase capable of methylating membrane-bound methyl-accepting chemotaxis proteins (MCPs) of a chemotaxis mutant was purified to homogeneity. MCPs are normally unmethylated in this strain. Results of gel filtration chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicate that the enzyme is a 30,000 molecular weight monomer.