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A:
From the looks of your output, it seems like you were using a text editor to copy the file to the clipboard, then using pbcopy to paste it into an editor (e.g. pbcopy /tmp/test.txt). Instead, you should be using a “real” command line utility like cut or cat to copy.
Try replacing pbcopy with cut.
cut -f 2 /dev/ttyUSB0 > /tmp/test.txt
Inactivation of matrilysin, a matrix metalloproteinase and basement membrane sheddase, prolongs full-thickness wound healing in mice.
In contrast to physiological epidermal wound repair in rodents, full-thickness skin wounds in humans heal by contraction rather than regeneration. Because contraction depends on the degradation of the basement membrane, our aim was to determine whether matrilysin, a matrix metalloproteinase and basement membrane sheddase, participates in full-thickness wound repair. We used intradermal excisional wounding in matrilysin-null mice and their wild-type littermates and a full-thickness wound model in matrilysin-null mice and their wild-type littermates. Excisional wounds healed without a scar in both strains of mice with the exception of wounds inflicted in matrilysin-null mice. Contraction was profoundly retarded, the epidermis remained acellular in thickened dermis, and hair follicles and sebaceous glands persisted in matrilysin-null mice and their wild-type littermates. The same was true for full-thickness wounds. Matrilysin is not required for the initial degradation of the basement membrane, because matrix metalloproteinase-2 activity was identical in both skin and gingiva. In both wound types, selective basement membrane sheddase-3 activity was reduced in matrilysin-null mice and their wild-type littermates, but the reductions were smaller than expected. When mice were treated with a pharmacologic
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