Cell phones and electronic appliances and devices are inseparable
from most people in modern society and the electromagnetic
field (EMF) from the devices is a potential health
threat. Although the direct health effect of a cell phone and its
radiofrequency (RF) EMF to human is still elusive, the effect
to unicellular organisms is rather apparent. Human microbiota,
including skin microbiota, has been linked to a very
significant role in the health of a host human body. It is important
to understand the response of human skin microbiota
to the RF-EMF from cell phones and personal electronic
devices, since this may be one of the potential mechanisms
of a human health threat brought about by the disruption
of the intimate and balanced host-microbiota relationship.
Here, we investigated the response of both laboratory culture
strains and isolates of skin bacteria under static magnetic
field (SMF) and RF-EMF. The growth patterns of laboratory
cultures of Escherichia coli, Pseudomonas aeruginosa,
and Staphylococcus epidermidis under SMF were variable
per different species. The bacterial isolates of skin microbiota
from 4 subjects with different cell phone usage history also
showed inconsistent growth responses. These findings led us
to hypothesize that cell phone level RF-EMF disrupts human
skin microbiota. Thus, the results from the current study lay
ground for more comprehensive research on the effect of
RF-EMF on human health through the human-microbiota
relationship.
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Streptomyces fradiae protease inhibitor (SFI) was purified effectively by preparative isoelectric focusing and hydroxyapatite chromatography. The molecular weight of SFI was estimated to be 1.7 kDa by SDS-PAGE and 1.8 kDa by molecular sieving HPLC. One hundred and sixty amino acid residues were determined from which molecular weight of SFI was calculated to be 17.054 Da and carbohydrate residue was not detected. SFI was calculated to be 17,064 Da and carbohydrate residue was not detected. SFI was a monomeric protein with two reactive sits, of which isoelectric point was pH 4.1. N-terminal amino acid sequence of SFI had homology with SSI (Streptomyces subsilisin inhibitor) and other protease inhibitors produced by Streptomyces.