6-Aminocaproic acid hydrochloride

Aminobenzophenone, 32, 8 c-Aminocaproic acid, 32, 13 6-Aminocaproic acid hydrochloride, 32, 13... 

Amide reduction with lithium aluminum hydride, 39, 19 Amine oxide formation, 39, 40 Amine oxide pyrolysis, 39, 41, 42 -Aminoacetanilide, 39, 1 Amino adds, synthesis of, 30, 7 2-Amino-4-anilino-6-(chloro-METHYl) -S-TRIAZINE, 38, 1 -Aminobenzaldehyde, 31, 6 hydrazone, 31, 7 oxime, 31, 7 phenylhydrazone, 31, 7 > -Aminobenzoic add, 36, 95 2-Aminobenzophenone, 32, 8 c-Aminocaproic acid, 32, 13 6-Aminocaproic acid hydrochloride,... 

The resulting -aminocaproic acid hydrochloride is treated in a manner similar to that used in the preparation of df-alanine (Org. Syn. Coll. Vol. i, 20). The hydrochloride is dissolved in r 1. of water in a 1.5-I. beaker and treated successively with 50 g. of powdered litharge, 25 g. of powdered litharge, 5 g. of freshly precipitated lead hydroxide, 25 g. of powdered silver oxide (Note 2), and finally hydrogen sulfide. During this procedure, the original volume is maintained by the addition of small amounts of water. 

The resulting e-aminocaproic acid hydrochloride is converted into the amino acid by means of a column containing Amberlite IR-4B resin (Note 2) ... 

The solid -aminocaproic acid hydrochloride is dissolved in 1 1. of distilled water. This solution is passed through the column (downflow) and followed by at least 21. of distilled water (Note 5). 

Aminoacetic Acid, 4, 31 -Aminobenzoic acid, 7, 59 -Aminobenzophenone, 7, 26 -Aminocaproic Acid, 4, 3 1, 4-Aminonaphthol Hydrochloride,... 

Acetorphine Hydrochloride Medroxyprogesterone Acetate Niflumic Acid Aminocaproic Acid Doxorubicin Hydrochloride Diphenylpyraline Hydrochloride... 

The use of buffer solutions is usually advisable for accurate control of the pH of solutions used in spectrophotometric titrations, since the solutions will usually be so dilute (because of the relatively high protein or peptide absorptivity) as to offer little self-buffering. The usual buffers for the pH range from 9 to 13, i.e., borate, glycinate, phosphate, lysine, -aminocaproic acid, etc., are generally transparent through the 2950 A phenolate band. Buffer systems composed of piperidine (pK, 11) and its hydrochloride have been used to avoid the use of multivalent anions in the spectrophotometric titration of ribonuclease (Klee and Richards, 1957), but no other advantage is apparent for this system. 

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