Fant en tråd på et annet forum som beskriver hvordan man kan utvinne DMT fra melk 
Nå kan man vel strengt tatt utvinne DMT fra pusekatter også, men melk er jo både billig og lett tilgjengelig. Har veldig liten erfaring med hobbykjemi, så lurer på hva dere mer erfarne sier om dette? Gjennomførbart, for komplisert til at det er verd strevet, bare BS, etc etc... Med fare for å bryte god forumskikk poster jeg hele tek'en for enkelhets skyld. Tek'en er skrevet av Noen Som Ikke Er tip på drugs-forum. Tek'en har han selvsagt ikke skrevet selv, den er basert på en drømmevisjon blekkspruten hans hadde en dag
Here we go:
Har du lest helt hit, er jeg litt imponert 
Nå kan man vel strengt tatt utvinne DMT fra pusekatter også, men melk er jo både billig og lett tilgjengelig. Har veldig liten erfaring med hobbykjemi, så lurer på hva dere mer erfarne sier om dette? Gjennomførbart, for komplisert til at det er verd strevet, bare BS, etc etc... Med fare for å bryte god forumskikk poster jeg hele tek'en for enkelhets skyld. Tek'en er skrevet av Noen Som Ikke Er tip på drugs-forum. Tek'en har han selvsagt ikke skrevet selv, den er basert på en drømmevisjon blekkspruten hans hadde en dag
Here we go:
Stage 1
L-Tryptophan From Milk
To 1 liter of milk, from which the cream has been largely separated (by simple skimming), 0.05 M hydrochloric acid is slowly added, with stirring through a capillary tube extending to the bottom of the beaker. The addition is continued until the solution attains a pH of 4.6 (casein exists in milk in the form of a calcium derivative; pH 4.6 is the isoelectric point of free casein, which is soluble to the extent of only 0.11g/L water). Approximately 1 L of acid is required; the separation of the casein is practically complete at this point. Three liters of water is then added, stirring is discontinued, and the flocculent precipitate of casein is allowed to settle in the refrigerator for twelve to twenty-four hours. The clear supernatant liquid which contains soluble proteins and salts is removed as completely as possible by siphoning; the precipitate is collected on a suction funnel and washed with cold distilled water until the washings are free of calcium (test with ammonium oxalate)
The casein, which is contaminated with calcium phosphate and fats; is filtered to as small a volume as possible (about 500 mL) and transferred to a 2000ml beaker. It is then treated with 0.1 M sodium hydroxide, the alkali being added slowly and with stirring through a capillary extending to the bottom of the beaker (it is important to avoid a local excess of alkali, which would tend to denaturate the casein). The addition of alkali is continued until the pH of the mixture reaches 6.3 (at this pH sodium caseinate is largely dissolved, whereas calcium caseinate is largely undissolved); 100-150 mL of the alkali is required. At this pH the casein is completely in solution in the form of its sodium salt; fats, calcium phosphate, and any calcium caseinate remain undissolved. Care must be taken not to add more alkali than is necessary to bring the pH to the above point. The milky solution is filtered through a thick layer (10-15 mm.) of filter paper pulp tightly packed upon a suction funnel. The filtrate may be slightly opalescent; if it is less clear it is again filtered through a fresh layer of pulp.
The filtrate is brought to a pH of 4.6 with 0.05 M hydrochloric acid just as in the original precipitation, the necessary amount of acid being determined by titration of an aliquot portion, diluted fivefold, with 0.01 M hydrochloric acid, 220-250 mL of 0.05 M acid is required. As the reprecipitation progresses, the rate at which the acid is added is decreased in order to prevent precipitation at the tip of the capillary tube; vigorous mechanical stirring is, of course, essential. When the acidification is complete, 5000ml of cold distilled water is added and the flocculent precipitate allowed to settle in the refrigerator. After siphoning off the clear supernatant liquid, the casein is collected on a suction funnel, using hardened paper, washed with cold distilled water until free of chloride, sucked as dry as possible, and dried over calcium chloride in a vacuum desiccator. The yield is 23-29 g. of a colorless coherent product which may readily be pulverized in a mortar.
L-Tryptophan
In an 8 Liter bottle is placed 600g of commercial casein (coarse powder), which is then covered with about 3200 mL of tap water at 37°C. The bottle is shaken until all the casein is moistened. A solution of 60 g. of anhydrous sodium carbonate and 6 g. of sodium fluoride (to inhibit oxidase enzymes present) in 1 L of water at 37°C is added. A thin paste of 20 g. of commercial pancreatin in 100 mL of water (37°C) is poured in. The mixture is covered with a layer of toluene (80 mL), diluted to 6 L, stoppered, shaken thoroughly, and placed in a warm room or bath at 37°C. After four or five days, with daily shakings, most of the casein is in solution and chalky masses of tyrosine begin to separate. After five days, a second 20-g. portion of pancreatin in 100 mL of water is added. After twelve days, the bottle is cooled in an icebox overnight and the undissolved material is filtered off (This filtration may be slow. Büchner funnels of 20-cm. diameter are best used; the material from a single filling is allowed to suck dry and the filter paper then changed).
The filtrate (6.9-7 L) is measured into a 16-L stone jar, and for every liter there is added 163 mL of dilute sulfuric acid (one volume of 95 per cent sulfuric acid and one volume of water, cooled to room temperature). The first part of the acid must be added cautiously on account of the liberation of carbon dioxide. The tryptophan is precipitated by adding a solution of 200 g. of mercuric sulfate (Note 5) in a mixture of 1860 mL of water and 140 mL of 95 per cent sulfuric acid. After standing for twenty-four to fortyeight hours, the clear liquid is siphoned out and the yellow precipitate is filtered and washed with a solution of 100 mL of concentrated sulfuric acid in 1.9 L of distilled water containing 20 g. of mercuric sulfate, until the filtrate is colorless and Millon's test is atypical; about 1.5 L is necessary. The precipitate is washed with three successive 500-mL portions of distilled water to remove most of the sulfuric acid.
The moist precipitate (120-130 g) is suspended with mechanical stirring in 1.2-1.3 L of distilled water, and a hot, 20 per cent aqueous solution of barium hydroxide is added until the mixture is permanently alkaline to phenolphthalein (about 120 mL is required). A rapid stream of hydrogen sulfide is passed in with stirring until the mercury is completely precipitated. The precipitate is filtered and washed with water until a sample of the washings gives a negative test for tryptophan with bromine water. The barium is removed from the combined filtrate and washings by adding the exact amount of dilute sulfuric acid and filtering. The filtrate is concentrated under reduced pressure to about 80 mL.
The tryptophan is extracted from the aqueous solution by repeated shaking in a separatory funnel with 25-mL quantities of n-butyl alcohol; water is added from time to time to keep the volume approximately constant. The butyl alcohol extract is distilled under reduced pressure. After the water present has distilled, the tryptophan precipitates in the distilling flask and may cause bumping. When all the water has been removed, as is indicated by non-formation of drops on the side of the condenser, the distillation is stopped and, after cooling, the tryptophan is filtered and washed with a little fresh butyl alcohol. Such extractions and distillations are continued until the quantities of tryptophan obtained are negligibly small.
The tryptophan so produced (7-8 g.) varies somewhat in quality in different runs. It is purified by recrystallization from 60 mL of dilute alcohol (two volumes of 95% alcohol to one volume of water), filtering from the hot solution an appreciable quantity of insoluble matter, and subjecting this to a second extraction with an additional 10 mL of aqueous alcohol. The solution is decolorized by the addition of 1 g. of Norite and allowed to stand in the icebox; the silvery leaflets of tryptophan are filtered and washed successively with cold 70 per cent, 80 per cent, 95% alcohol, and, finally, with a little ether. Less than half the tryptophan is obtained in each crystallization. The yield of pure tryptophan is 4.0-4.1 g., together with under 0.1 g of less pure product.
Stage 2
Decarboxylation of Tryptophan in Diphenylmethane
A suspension of L-tryptophan (250 mg) in warm diphenylmethane (10 g) was gently refluxed in a stream of nitrogen for 5-20 min until no more evolution of carbon dioxide was observed. After cooling, the clear pale yellow reaction mixture was treated with a benzene solution (20 ml) saturated with dry hydrogen chloride. The resulting precipitate was collected by filtration, washed with n-hexane and dried to afford crude tryptamine hydrochloride (223 mg, 93%) which was recrystallised from ethanol/ethyl acetate to yield tryptamine hydrochloride (151 mg, 63%) as colorless needles, mp 248-249°C.
Stage 3
DMT (from tryptamine and ethyl formate)
A suspension of 1.0 g tryptamine in 50 mL ethyl formate was held at reflux for 15 h during which time the mixture became homogeneous. The volatiles were removed under vacuum, yielding an oily residue of the formamide. This may be purified by distillation but this unpurified product can serve satisfactorily in the following reaction. This residue was dissolved in 50 mL anhydrous THF and added, dropwise, to a solution of 1.0 M LAH in THF (40 mL, 40 mmole) which had been diluted with another 50 mL THF. After the addition was complete the reaction mixture was heated under reflux for 15 hours. Reflux was continued as a solution of 40 mL 1.0 M freshly distilled ethyl formate in THF was added dropwise over the course of 2 h. Heating was discontinued and the reaction mixture was quenched by the addition of excess solid sodium sulfate decahydrate at room temperature. The reaction mixture was filtered and the filtrate was concentrated under vacuum to yield 1.15 g pure N,N-dimethyltryptamine as an oil which solidified upon storage in the freezer. The material can be recrystallized from hexane to give white crystals with a mp 67 °C.
L-Tryptophan From Milk
To 1 liter of milk, from which the cream has been largely separated (by simple skimming), 0.05 M hydrochloric acid is slowly added, with stirring through a capillary tube extending to the bottom of the beaker. The addition is continued until the solution attains a pH of 4.6 (casein exists in milk in the form of a calcium derivative; pH 4.6 is the isoelectric point of free casein, which is soluble to the extent of only 0.11g/L water). Approximately 1 L of acid is required; the separation of the casein is practically complete at this point. Three liters of water is then added, stirring is discontinued, and the flocculent precipitate of casein is allowed to settle in the refrigerator for twelve to twenty-four hours. The clear supernatant liquid which contains soluble proteins and salts is removed as completely as possible by siphoning; the precipitate is collected on a suction funnel and washed with cold distilled water until the washings are free of calcium (test with ammonium oxalate)
The casein, which is contaminated with calcium phosphate and fats; is filtered to as small a volume as possible (about 500 mL) and transferred to a 2000ml beaker. It is then treated with 0.1 M sodium hydroxide, the alkali being added slowly and with stirring through a capillary extending to the bottom of the beaker (it is important to avoid a local excess of alkali, which would tend to denaturate the casein). The addition of alkali is continued until the pH of the mixture reaches 6.3 (at this pH sodium caseinate is largely dissolved, whereas calcium caseinate is largely undissolved); 100-150 mL of the alkali is required. At this pH the casein is completely in solution in the form of its sodium salt; fats, calcium phosphate, and any calcium caseinate remain undissolved. Care must be taken not to add more alkali than is necessary to bring the pH to the above point. The milky solution is filtered through a thick layer (10-15 mm.) of filter paper pulp tightly packed upon a suction funnel. The filtrate may be slightly opalescent; if it is less clear it is again filtered through a fresh layer of pulp.
The filtrate is brought to a pH of 4.6 with 0.05 M hydrochloric acid just as in the original precipitation, the necessary amount of acid being determined by titration of an aliquot portion, diluted fivefold, with 0.01 M hydrochloric acid, 220-250 mL of 0.05 M acid is required. As the reprecipitation progresses, the rate at which the acid is added is decreased in order to prevent precipitation at the tip of the capillary tube; vigorous mechanical stirring is, of course, essential. When the acidification is complete, 5000ml of cold distilled water is added and the flocculent precipitate allowed to settle in the refrigerator. After siphoning off the clear supernatant liquid, the casein is collected on a suction funnel, using hardened paper, washed with cold distilled water until free of chloride, sucked as dry as possible, and dried over calcium chloride in a vacuum desiccator. The yield is 23-29 g. of a colorless coherent product which may readily be pulverized in a mortar.
L-Tryptophan
In an 8 Liter bottle is placed 600g of commercial casein (coarse powder), which is then covered with about 3200 mL of tap water at 37°C. The bottle is shaken until all the casein is moistened. A solution of 60 g. of anhydrous sodium carbonate and 6 g. of sodium fluoride (to inhibit oxidase enzymes present) in 1 L of water at 37°C is added. A thin paste of 20 g. of commercial pancreatin in 100 mL of water (37°C) is poured in. The mixture is covered with a layer of toluene (80 mL), diluted to 6 L, stoppered, shaken thoroughly, and placed in a warm room or bath at 37°C. After four or five days, with daily shakings, most of the casein is in solution and chalky masses of tyrosine begin to separate. After five days, a second 20-g. portion of pancreatin in 100 mL of water is added. After twelve days, the bottle is cooled in an icebox overnight and the undissolved material is filtered off (This filtration may be slow. Büchner funnels of 20-cm. diameter are best used; the material from a single filling is allowed to suck dry and the filter paper then changed).
The filtrate (6.9-7 L) is measured into a 16-L stone jar, and for every liter there is added 163 mL of dilute sulfuric acid (one volume of 95 per cent sulfuric acid and one volume of water, cooled to room temperature). The first part of the acid must be added cautiously on account of the liberation of carbon dioxide. The tryptophan is precipitated by adding a solution of 200 g. of mercuric sulfate (Note 5) in a mixture of 1860 mL of water and 140 mL of 95 per cent sulfuric acid. After standing for twenty-four to fortyeight hours, the clear liquid is siphoned out and the yellow precipitate is filtered and washed with a solution of 100 mL of concentrated sulfuric acid in 1.9 L of distilled water containing 20 g. of mercuric sulfate, until the filtrate is colorless and Millon's test is atypical; about 1.5 L is necessary. The precipitate is washed with three successive 500-mL portions of distilled water to remove most of the sulfuric acid.
The moist precipitate (120-130 g) is suspended with mechanical stirring in 1.2-1.3 L of distilled water, and a hot, 20 per cent aqueous solution of barium hydroxide is added until the mixture is permanently alkaline to phenolphthalein (about 120 mL is required). A rapid stream of hydrogen sulfide is passed in with stirring until the mercury is completely precipitated. The precipitate is filtered and washed with water until a sample of the washings gives a negative test for tryptophan with bromine water. The barium is removed from the combined filtrate and washings by adding the exact amount of dilute sulfuric acid and filtering. The filtrate is concentrated under reduced pressure to about 80 mL.
The tryptophan is extracted from the aqueous solution by repeated shaking in a separatory funnel with 25-mL quantities of n-butyl alcohol; water is added from time to time to keep the volume approximately constant. The butyl alcohol extract is distilled under reduced pressure. After the water present has distilled, the tryptophan precipitates in the distilling flask and may cause bumping. When all the water has been removed, as is indicated by non-formation of drops on the side of the condenser, the distillation is stopped and, after cooling, the tryptophan is filtered and washed with a little fresh butyl alcohol. Such extractions and distillations are continued until the quantities of tryptophan obtained are negligibly small.
The tryptophan so produced (7-8 g.) varies somewhat in quality in different runs. It is purified by recrystallization from 60 mL of dilute alcohol (two volumes of 95% alcohol to one volume of water), filtering from the hot solution an appreciable quantity of insoluble matter, and subjecting this to a second extraction with an additional 10 mL of aqueous alcohol. The solution is decolorized by the addition of 1 g. of Norite and allowed to stand in the icebox; the silvery leaflets of tryptophan are filtered and washed successively with cold 70 per cent, 80 per cent, 95% alcohol, and, finally, with a little ether. Less than half the tryptophan is obtained in each crystallization. The yield of pure tryptophan is 4.0-4.1 g., together with under 0.1 g of less pure product.
Stage 2
Decarboxylation of Tryptophan in Diphenylmethane
A suspension of L-tryptophan (250 mg) in warm diphenylmethane (10 g) was gently refluxed in a stream of nitrogen for 5-20 min until no more evolution of carbon dioxide was observed. After cooling, the clear pale yellow reaction mixture was treated with a benzene solution (20 ml) saturated with dry hydrogen chloride. The resulting precipitate was collected by filtration, washed with n-hexane and dried to afford crude tryptamine hydrochloride (223 mg, 93%) which was recrystallised from ethanol/ethyl acetate to yield tryptamine hydrochloride (151 mg, 63%) as colorless needles, mp 248-249°C.
Stage 3
DMT (from tryptamine and ethyl formate)
A suspension of 1.0 g tryptamine in 50 mL ethyl formate was held at reflux for 15 h during which time the mixture became homogeneous. The volatiles were removed under vacuum, yielding an oily residue of the formamide. This may be purified by distillation but this unpurified product can serve satisfactorily in the following reaction. This residue was dissolved in 50 mL anhydrous THF and added, dropwise, to a solution of 1.0 M LAH in THF (40 mL, 40 mmole) which had been diluted with another 50 mL THF. After the addition was complete the reaction mixture was heated under reflux for 15 hours. Reflux was continued as a solution of 40 mL 1.0 M freshly distilled ethyl formate in THF was added dropwise over the course of 2 h. Heating was discontinued and the reaction mixture was quenched by the addition of excess solid sodium sulfate decahydrate at room temperature. The reaction mixture was filtered and the filtrate was concentrated under vacuum to yield 1.15 g pure N,N-dimethyltryptamine as an oil which solidified upon storage in the freezer. The material can be recrystallized from hexane to give white crystals with a mp 67 °C.
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