how to dissolve gelatin capsules in suitable solvent for GC-MS ananlysis?
538173
I don't think gelatin is amenable to GC-MS analysis.  Gelatin is a protein which is non-volatile.  It would be better to use HPLC or HPLC-MS.
29066
The answer should be Hydrolysis.
46637
Prozymes (protein portion of the enzyme) require a spacific temperature range to operate properly.  At both ends of this spacific operating range there are laten temperature ranges.  These ranges render the prozyme ineffective but still redeemible. Even further from the spacific temp range, outside the laten temp ranges are denaturation temps.  These are the temps where the prozyme is damaged to the point where it can never again function properly.  The heating methode of denaturation is usually used only when pH of the resulting supernatant will be measured.  Otherwise one could simplely titrate to the desired pH using a more effective methode. \n\nAs not to disperce the debriss of denaturation into your solution the Acid coagulum methode is perhaps the best way.  This can be achieved by adding to the solution just enough glaceral acitic acid untill the protein stops gelling.  The solution should actually become less turbit.  Finally, use ETOH to counter titrate to the desired pH.  Remember countertitration makes water (H2O) in your solution so don't add excessive acid to begin with. E-mail me with your results.  I am interested.
117711
>>>1. Plant medicine\n>>>2. Dry completely\n>>>3. Grinding\n>>>4. Methanol extraction\n>>>5. Filtration using Watmann No. 5 filter paper\n>>>5. Concentration with rotary evaporator\n>>>6. Suspend in distilled water\n>>>7. Partitioning\n>>> 1) partition with hexane\n>>> 2) partition with n-butanol
1038474
http://www.chem.purdue.edu/gchelp/howtosolveit/Solutions/concentrations.html
712851
Dissolve 3.2 g of KMnO4 in water to make 500 mL final volume. This will be 0.04M KMnO4 solution.
174475
mix it...let NaCl dissolve in water...then let the mmixture evaporate or perhaps bring the mixture into a boil 'til you can see the formation of crystals...   try it... i've encountered such experiment in my chemistry class... im not quite certain of the procedures though...it's two years ago...cant remember it well...^_^
694165
go get some kind of pill I used alka - seltzers \nget like 5 diff. liquids and time how long they take t o dissolve in each \nREALLY EASY!!!!!\n\n\n\n\nI used like water, root beer, other pops, orange juice and some other stuff. they took like 20 - 30 secs each
57120
Well, you'd have to specify what you are trying to dissolve.  Many plastics are soluble in several solvents... N-Methylpyrrolidone being a good one.  Solvents generally do not attack metals, unless they contain water.  I would steer away from an acid or a base.  Can you say what you're thinking of?  If so, email me at connecticutpoet37@yahoo.com
512002
Yup, non-polar solvents.  If acetone, alkanes, or toluene don't work, then go with petroleum ether(hist. ligroin) that dissolves alot of things.
665494
It can be made by dehydration of acrylamide\nCH2=CH-C(O)NH2 --> CH2=CH-CN + H2O\nP2O5 is a good reagent for that.
840473
Need more specifics as to your problem.\n\nHowever, I assume you are trying to do a quantitation on a UV or vis absorbing substance.\n\nMake up  a set of standards of known concentration of your analyte in the solvent you will be analyzing in.  Then do some scans over the whole wavelength range. \n\nUsually pick the wavelength at the top of the largest absorbance peak, unless that is a wavelength which will have interferences from other substances present.  If so, then pick a wavelength with good absorbance that is not subject to such interference.
721414
Proteins were precipitated with an equal volume of 20% (w/v) trichloroacetic acid and washed three times with 4 ml of an ethanol/ethyl acetate mixture (1:1). Washings were achieved by mechanical disruption of pellets in the washing solution using a small spatula, and re-pelleting by centrifugation at 6000 g for 5 min. Finally, the precipitates were dissolved in 6 M-guanidine-HCl solution.Ref:Cell. Biochem. Func.(2006)24:79-85.
882103
Ok, what I normally do is to digest the plasmid with RE, digesting as much as possible for long time (even over-night). Then, without any purification I treat my digestion with CAP (calf alkaline phosphatase) for one hour at 37C. This phosphatase is generally versatile and works in any buffer, but you might want to check with the manufacturer's instructions for buffer compatibility.\nAfter de-phosphorylation, I make a 1% agarose in TAE with a comb with big wells. If you do not have one, you can tape 2 "teeth" together to make a bigger well. Make sure you add Ethidium Bromide to the gel. I run all my digest on the gel for 1 hour or so at medium volt (so that the gel does not become hot) and then cut the band  and purify with a gel purification kit (Qiagen has a very good one). The kit has columns that bind DNA from which your plasmid can be eluted - If you don't have a lot, elute with a small volume of H2O (DNAse-free!).\n\nThe advantage of running the gel and purifying the band is that you get rid of all un-digested plasmid which would be useless in the ligation but that would definitely be transformed into your E.coli (quite well, as well!).\nAlso, if you are cutting and purifying an insert from a different plasmid, you can run vector and insert side by side to see in which proportion to organise your ligation. If you don't have a lot material, try "Rapid Ligation Kit" by Roche. It works at room temperature within 1 hour.\n\nHope this helps!\nGood luck
995016
You need to extract the sugar from the solution.\n\nExtract it by using a solvent where sugar dissolves but the salt won't.  If the sugar dissolves more in your other solvent, the extraction will be faster.  You might try isopropyl alcohol (2-propanol or IPA) as the solvent.\n\nStep by step:\n\nGet an separation funnel of the right size.\n\nPour in your solution.\n\nPour in the IPA.  Confirm which layer is the aqueous (bottom) and which is the organic layer.)\n\nMix the two layers by gently shaking and swirling.\n\nSeparate the two layers, by decanting the top layer (fastest).\n\nRepeat w/ fresh IPA.\n\nIf you want the sugar, then boil off or rotovaporate your IPA.\n\nYou'll have to check or determine the solubility of sugar in IPA (can't find it in my CRC Handbook, but I don't have alot of time).
755540
The best solvent for all albumins (including egg albumin) is buffered water.  The key is to not allow acid or bases or heat to denature any of the albumin.  Denaturing makes the protein insoluble.\n\nWarm (not hot or cold) water near pH of 7 is best.  The usual solubility is about one gram of albumin per 10 cc or mL of water.
1102382
You can dissolve it in water. Upto 7.4 g dissolves in 100 mL of water.  This solution will be acidic.