i have various 2c-* drugs and i have been wanting to form them into a pill. i find it hard to find a pill press and im also wondering if a bonding agent is needed. is food dye a reliable bonding agent.... any helpful answers gladly taken.
you should put this in the synthetic drug section, i think it would get more views.... im also curious about how to go about doing this properly..
i have done capsules they are easy as shit. but im more interested in making pills. im also thinking if food dye is a good bonding agent, than you can make fuckin red, green, or whatever pills of any 2c
What about some kind of liquid that when cools or dries becomes hard (like candy for example?) You could mix the 2c's in at the correct ratios. Then you pour this liquid before it cools/dries into a pill mold so that when hardened, they maintain the correct shape?
mix in some sugar and moisten slightly. it will bond and harden as it dries easy example: lick the backs of 2 gummy bears and hold em together for a few minutes. they will stick to eachother and be surprisingly difficult to seperate.
Binders tend to be micronized sugars. Lactose 'n cellulose are the most common, but others will work. Sometimes, a food-grade wax has been added - usually as a coating, but a wax matrix will act as a ghetto "time release," and is allegedly used as such in some pharmaceuticals. Once you get real good you can start bias-dying your pills, by stamping with warm/molten wax, hosing it down with opaque water-based food-grade dye, and then wiping off the wax with a spot of food-grade hexane or somesuch. Same principle as the black crayon + watercolor drawing method...
I don't think food coloring would work since 2c-Xs can be dissolved in water it would just give you a pile of half absorbed red mess.
yeap..... if you need a pill, why not take a asprin or something low like children tylonol.. mush it all up add 2cs to it.... and allow it to dry... weve put liquid acid on baby tylonol.. like duh, transporting it is much easier like that, even if you got pulled over and they found it, its in the same bottle and its not deformed much to be noticed, dont dose the number side... Not sure how it will effect the acid either... but you asked a whole different question.... SInce tylonol isnt that bad at low levels Id try it... make a mold out of plastic or steel.. stainless it will not stick. I dont think it will if you used some Pam on it.. LOL.
What aer you, plain fucking retarded or deliberately trying to kill the boy? Cross-competitive of cytochrome metabolism mean anything to you? How about serotonin syndrome? HPPD? Chemical hepatitis?
for real homes.. Dont try to come here on a fucking guest tag with like 9 post under you belt making like you know what the fuck your talking about?? One your not even on topic.. 2 your got 9 post... If the mofo knows how to measure 2ce out then he'll be fine so what the fuck are you talking about? Tell me for shits a giggles>.. PLEASE.. 1: The substrate binds to the active site of the enzyme, in close proximity to the heme group, on the side opposite to the peptide chain. The bound substrate induces a change in the conformation of the active site, displacing a water molecule from the distal axial coordination position of the heme iron[5], changing the state of the heme iron from low-spin to high-spin[6]. This gives rise to a change in the spectral properties of the enzyme, with an increase in absorbance at 390 nm and a decrease at 420 nm. This can be measured by difference spectrometry and is referred to as the "type I" difference spectrum (see inset graph in figure). Some substrates cause an opposite change in spectral properties, a "reverse type I" spectrum, by processes that are as yet unclear. Inhibitors and certain substrates that bind directly to the heme iron give rise to the type II difference spectrum, with a maximum at 430 nm and a minimum at 390 nm (see inset graph in figure). If no reducing equivalents are available, this complex remains stable, allowing the degree of binding to be determined from absorbance measurements in vitro[7] 2: The change in the electronic state of the active site favours the transfer of an electron from NAD(P)H[8]. This takes place via the electron transfer chain, as described above, reducing the ferric heme iron to the ferrous state. 3: Molecular oxygen binds covalently to the distal axial coordination position of the heme iron. The cysteine ligand is a better electron donor than histidine, with the oxygen consequently being activated to a greater extent than in other heme proteins. However, this sometimes allows the bond to dissociate, the so-called "decoupling reaction", releasing a reactive superoxide radical, interrupting the catalytic cycle[5]. 4: A second electron is transferred via the electron-transport system, either from cytochrome P450 reductase, ferredoxins, or cytochrome b5, reducing the dioxygen adduct to a negatively charged peroxo group. This is a short-lived intermediate state. 5: The peroxo group formed in step 4 is rapidly protonated twice by local transfer from surrounding amino-acid side chains, releasing one mole of water, and forming a highly reactive iron(V)-oxo species[5]. 6: Depending on the substrate and enzyme involved, P450 enzymes can catalyse any of a wide variety of reactions. A hypothetical hydroxylation is shown in this illustration. After the product has been released from the active site, the enzyme returns to its original state, with a water molecule returning to occupy the distal coordination position of the iron nucleus. S: An alternative route for mono-oxygenation is via the "peroxide shunt": interaction with single-oxygen donors such as peroxides and hypochlorites can lead directly to the formation of the iron-oxo intermediate, allowing the catalytic cycle to be completed without going through steps 3, 4 and 5[7]. A hypothetical peroxide "XOOH" is shown in the diagram. C: If carbon monoxide (CO) binds to reduced P450, the catalytic cycle is interrupted. This reaction yields the classic CO difference spectrum with a maximum at 450 nm. Way off topic Clown.... Cut and paste and back up you shit...
with some baby tylonol yet to get a binder.. really Id read the lable on the box. Put together somekinda starch / sugar bonder and mix the 2ce.. Same thing.. Low levels of tylonol with 2ce. thats like mixing DXM with tylonol. Pill size dont matter ever see a true E pill.. some are huge.. but Im not sure of the measurement on th 2ce. But Im sure the OP is... I thinks thinks this is being cooked with 2ce.. of course youll have new compounds and radicals.. But not by mixing alone. Chemical Hep.. pttf.. usaully false positves can be avoided by fasting 24 hours.. Thats why they tell you to fast.
thats exactly what they do as I posted the info... more phamacuticals they add though.. whatever they think will get ppl high.. check dea web site for findings on pills reported to be E.. its interesting.
ouch...orison holdin it down.. magnesium stearate is the main component found in binders. but, my advice to the OP: don't try to buy a pill press. you might as well email the DEA with your address and intentions.
you know them guys that sell to corner gas station speed pills as E.. How the hell do they do it?? I wish I was in my 20s Id hit all the raves and cluds and make a mint.. guess I cant say shit though when I was coming up I was slinging hard that was straight soda. and the crackheads would come with 3-7 bucks for a hit all day.. made a fortune.. so I had my fun if yould call it that.. thanks polymer.. didnt have the info in front of me.. I didnt utse< lol.
lmao@UTFSE reminds me of the days I used to frequent the original hive, spring '00. i merely observed and didn't ask any questions
