You are missing the point. If you spend money on your business, it doesn't count as income. Good business owners don't decide how much money to spend on their business after they are done buying personal things.
I think it is you who seems to be missing the point. All money coming into your business counts as income, that's basic accounting. What you then have is gross income (total income before expenditures) then net income (income left over after spending on bills, new widgets, whatever).
What you also seem to be missing is that businesses and individuals have budgets. If they see that their spending is starting to outpace their income, they cut their spending accordingly. They don't instantly raise their prices or demand their bosses give them a raise.
The big three expenditures of the federal government are: Social Security, Medicare/caid & Defense (with Defense being the least of the 3). Together they make up ~64% of the federal budget, this is before salaries, pensions or other mandatory spending.
To put this into an analogy, you make 100k per year and are spending an extra 64k on top of your earnings
(for a total spending of 164k per year) on money to charities and buying guns.
My solution is "live within your means" and cut your spending down to only necessities until you get your debt (which is now at 1.6 million, to keep the analogy in the same ballpark) under control. Your solution is to go to your boss and demand a raise.
How does your solution make sense?
This post was edited on 12/6 at 12:29 pm