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Comment. Accuracies of ± 5 % are readily obtained by this method when the spot has distinct edges. If there is overlapping or if the spot is distorted, the method should not be used. The chief disadvantage of this method is the tediousness of the area determinations. * As methionine bleaches the PtI6 reagent, this amino acid is estimated from the area of the spot. , (log cJlog 1) = K Method IV: Elution of Spots This widely used procedure is based on the simple expedient of cutting out the section of the developed chromatogram which contains a single substance, removing the substance from the paper, and determining its amount in the e1utriate by an appropriate method.

O in 0·25NHCI at a wavelength of 515 m,u is preferable for these calibrations (Dr. W. G. Gordon, unpublished). ) is a neutral, stable detergent, which permits faster flow during elution. Dissolve 50 g of BRIJ 35 in 100 ml of H 20 for the stock solution. Both TG and the BRIJ 35 solution are added in the stated quantities to severa1litres of the buffer shortly before use, not to the 40 1. quantities that are to be stored. BRIJ 35 can be omitted if it interferes with the action of the fraction collecting device.

Method. Dilute an aliquot of the hydrolysate containing 10 mg of protein to 250 ml. Shake 10 ml of diluted solution with 1 g of Permutit for 10 min. Filter or decant and remove an aliquot containing 1O-80,ug of proline and dilute with water to 1·0 ml. Add 0·2 ml of H SP0 4, 2·0 ml of ninhydrin reagent and 2·0 ml of I-propanol. Heat in boiling water for 1 hr. Dilute to 10·0 ml with absolute ethanol and read against the reagent blank at 515 m,u. F. MICROBIOLOGICAL METHODS The historical development of amino acid assay by biological methods and the possible sources of error in these procedures are discussed by Block and Weiss (1946).

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