Letter | Published:

Chemical Nature of Human Brain Thromboplastin

Naturevolume 214pages197198 (1967) | Download Citation



IN 1958, Hecht et al.1 prepared a thromboplastin (TP) from rabbit brain dried with acetone according to Quick2. Inactive fractions containing protein with respect to blood coagulation were separated by repeated ultracentrifugation from a transparent, biuret negative lipid material which possessed the properties of a fully active thromboplastin. In a similar manner, Deutsch et al.3 prepared a purified, biuret negative TP from human brain. On further treatment with pyridine, however, two fractions were obtained. One of these was soluble in pyridine, free of protein, and exhibited only a weak promotion of clotting effect as is commonly the case with lipid activators4. It was considered to be the lipid moiety of the TP. The other fraction was insoluble in pyridine, inactive in blood coagulation, and according to Deutsch et al.3 the protein moiety of the TP. The authors assumed that the rabbit brain TP of Hecht et al.1 was identical with their preparation, and was thus a compound containing protein as well.

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    Hecht, E., Cho, M. H., and Seegers, W. H., Amer. J. Physiol., 193, 584 (1958).

  2. 2

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  1. Medical Department, University Hospital, Utrecht

    • E. HECHT


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