Between May 1979 and April 1983, 18 previously healthy African patients were hospitalized in Belgium with opportunistic infections (cryptococcosis, Pneumocystis carinii pneumonia, central-nervous-system toxoplasmosis, progressive cutaneous herpes simplex virus infection, disseminated cytomegalovirus infection, candidiasis, or cryptosporidiosis) or Kaposi's sarcoma, or with both. Ten of them died. During the same period five other patients were hospitalized with an illness consistent with a prodrome of the acquired immunodeficiency syndrome (chronic lymphadenopathy, fever, weight loss, and diarrhea). All patients tested had a marked decrease in helper T cells; an inversion of the normal ratio of helper to suppressor T cells, and a decreased or absent blastogenic response of lymphocytes to mitogens. Twenty patients had anergy. There was no evidence of an underlying immunosuppressive disease and no history of blood-product transfusion, homosexuality, or intravenous-drug abuse. This syndrome in patients originating in Central Africa is similar to the acquired immunodeficiency syndrome reported in American patients.

The phospholipid requirement for the optimal solubilization of carnitine acylcarnitine translocase from the inner membrane vesicles of rat liver mitochondria and for its reconstitution in liposomes was investigated. At the octylglucoside-solubilization step, the presence of cardiolipin proved superior to the other lipids tested. For reconstitution, a mixture having phosphatidylcholine, phosphatidylethanolamine and cardiolipin was found to be particularly effective. The requirement of cardiolipin at this step was met less effectively by other anionic phospholipids. Moreover, in intact mitochondria of rat liver and heart, the translocase activity was markedly inhibited by micromolar concentrations of doxorubicin, a specific cardiolipin-binding agent.Carnitine acylcarnitine translocase, involved in the transmitochondrial transport of carnitine and its esters, has been solubilized from inner membrane vesicles of rat liver mitochondria with octyl glucoside and reconstituted into asolectin liposomes using the octyl glucoside dilution method [l]. Continuing studies on the optimization of these procedures have revealed an esstential requirement of cardiolipin for the translocase activity. These are being described herein.

The photoreaction center from Rhodospirillum rubrum contains about 90% protein, 6% pigment, mere traces of lipids, and no cytochromes. It also contains at least 1 mol of ubiquinone and 1 iron atom per mol. Its three-component polypeptide chains were isolated by preparative electrophoresis, and their molar stoichiometry was established as 1:1:1. The amino acid composition of the photoreaction center from strain S1 and from its subunits is reported. The protein as a whole contains about 65% nonpolar residues, and the degree of hydrophobicity of its subunits is alpha less than beta less than gamma. The minimal molecular weight based on the extinction coefficient and on the amino acid content is 90 000. This corresponds to a half-cystine mole number of 6.

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