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IN the fifth chapter of Barcroft's book on haemoglobin he discusses its specificity, and suggests the possibility of more than one haemoglobin in the same blood, the differences being located in the globin part of the molecule. The curious change in "span" (i.e. the distance between the bands for oxy-and CO-hsemoglobin) in the blood of the same rabbit makes B arcr oft put the question, " Why and how should the globin of a rabbit's h&emoglobin alter on haemorrhage? "In limiting the problem to the unity and variability of hamoglobin in one kind of blood, especially in human blood, we find that most methods of research on the specificity of h&-moglobin are not sensitive enough to detect the presence of, say, 10 p.c. of a modified hamoglobin in 100 p.c. total. Only the estimation of the so-called alkali resistance, which gives enormous differences in blood of different species, might be sensitive enough. This paper describes the photo-electric measurement of the rate of denaturation of human h8Bmoglobin at pH about 12, as a means of differentiation between more than one kind of pigment in the same blood.METHOD. Von Kruger [1888, 1925, 1927], who first studied the rate of h&-moglobin denaturation in alkaline solutions ("Zersetzungszeit"), added 1/5 vol. N/4 NaOH to the solution of hemoglobin and measured the time from this moment to the visual disappearance of the typical absorption bands. In this way he found the very large differences in "Zersetzungszeit" in the haomoglobin of mammalian species, for instance for human blood 1 min., for rabbit's blood 30 min., for horse blood 80 mim., for ox blood 24 hours. A more exact study was made by Haurowitz PH. LXXX. 25