General properties of avian oxyhemoglobin

Abstract

The results of the general test for oxyhemoglobin obtained from avian blood cellsby tlae authors method, are as follows.l. Isoelectric point of avian oxyhemoglobinThe isoelectric point was determined by the direct method using fractional pre-cipitation at a controlled pH. It was found to be 7.0, 6.5, 5.9, and 5.3. There was aconsiderable difference in it between fowl and man.2. Rate of alkaline denaturation of avian oxyhemoglobinHemoglobin solutions were exposed to an alkali reagent at pH 12.7. Normal avianpigments became completely denative within one minute.At concentrations of 0.7, 1.0, and 1.8 g per dl, adult chicken hemoglobin was moreresistant than young chicken hemoglobin. At a concentration of 1.3 g per dl, however, young chicken hemoglobin was more resistant than adult chicken hemoglobin.In general, the amount of adult chicken hemoglobin wltich had not been denaturedin each hemoglobin solution ranging from 0.5 to 2.0 g per dl was smaller in sum totalthan that of young chicken hemoglobin.3. Absorbancy of avian hemoglobin derivativesThe range of wave length for the intense absorption of avian hemoglobin deriva-tives was much the same as determined for that of human hemoglobin derivatives. Itwas as follows.(a) Hb0r : 418, 550, and 586 Illp(b) IIbC0 : 403, 550, and 590 Illjt(c) met Hb : 410, 505, and 640 Illjt, 4. Disc electrophoretic patterns of normal avian and mammalian hemoglobinThe disc electrophoretic behavior was compared between avian hemoglobin andhemoglobin of a given mammalian species. As was illustrated previously, avian oxy-hemoglobin revealed 10 components on disc electrophoretic analysis.Component 4-d, moving relatively fast toward the cathode, occupied the greater partof avian oxyhemoglobin. The properties of this component were unknown. Thiscomponent was identical with the corresponding one of mammalian hemoglobin, exceptcalf and goat one. It is justified in saying that this component may be regarded as onespecific to the ruminant.The greater part of mammalian hemoglobin is occupied by components