Abstract
Summary
1. It has been demonstrated that the Rh antigen is quite different in character from the A and B substances as found in stroma from human erythrocytes. The Rh factor is particularly sensitive to thermal inactivation and is destroyed by a few minutes exposure to 56°C while the A and B substances remain intact. The inactivation by heat in the presence of moisture and the absence of oxygen suggests protein denaturation as the basis for its destruction.
2. Erythrocyte stroma has been fractionated into 2 parts; (1) a protein previously described and called stroma tin, and (2) a new lipoprotein which we call elinin. The Rh specificity is associated with the elinin.
3. An ether-soluble fraction has been separated from elinin which is characterized by a higher content of the Rh factor and a lower content of A and B substances. The Rh substance present in the ether solution which inhibits the anti-Rh serum showed an increased thermostability.
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