ABSTRACT
PURPOSE: To investigate which muscular maneuvers provide larger electric activity (EA) of the suprahyoid (SH) and infrahyoid (IH) muscles to be used as surface electromyography (SEMG) signal normalization reference. METHODS: The electrical potentials of the SH and IH muscles of 12 subjects were evaluated using six muscular maneuvers, involving the position of the tongue and effort. It was selected as maximum voluntary sustained activity maneuver, the one having the minor coefficient of variation and the smallest value for each muscle group. The EA signal was converted using the root mean square in microvolts. It was considered then the maximum signal of each maneuver as the difference between the mean of three measures and the resting potential. RESULTS: The maneuvers that provided higher mean potentials with minor coefficient of variation and smallest P value were incomplete swallowing (IS) with effort (mean potential equal to 56.73±8.68 with coefficient of variation of 15.30%) in SH group, and tongue retracted with mouth open (TROM, mean potential equal to 46.57±7.83 with coefficient of variation of 16.81%) in IH group. CONCLUSION: The IS with effort and TROM maneuvers should be considered for signal normalization in these muscles, respectively, and may provide conditions for using the SEMG in voice clinic. SIGNIFICANCE: The use of normalization standards in researches of SH and IH muscles in the voice area will allow comparisons among future works.
Subject(s)
Deglutition , Electromyography , Isometric Contraction , Laryngeal Muscles/physiology , Signal Processing, Computer-Assisted , Tongue/physiology , Action Potentials , Adolescent , Adult , Electromyography/standards , Female , Humans , Male , Middle Aged , Movement , Reference Values , Volition , Young AdultABSTRACT
Omp-28 isolated from Salmonella enterica serovar typhi presented a subunit molecular mass of 9,632 Da by MALDI-TOF MS. It was denatured, S-alkylated, and 1) directly submitted to Edman sequencing, 2) cleaved with CNBr, and 3) hydrolyzed either with endoproteinase Glu-C or Asp-N. The major CNBr peptide containing the C-terminal portion of Omp-28 was isolated by tricine-SDS-PAGE and electroblotted whereas Omp-28 enzymatic peptides were isolated by C18-RP-HPLC. All peptides were sequenced. This approach allowed the elucidation of the complete primary structure of Omp-28. Its amino acid sequence is identical to that deduced from part of the DNA of the "putative periplasmic transport protein" of either S. enterica serovar typhimurium and a multiple drug resistant S. enterica serovar typhi. Omp-28 homologous protein sequences were also deduced from Escherichia coli and Yersinia pestis genomic DNA. All proteins had their secondary structures predicted. Immunogold cytochemistry indicated that Omp-28 is found on the bacterium outer membrane.