Seven new red-cell pyruvate kinase (PK) variants were characterized by the methods recently recommended by the International Committee for Stanardization in Haematology. The cases were all true homozygote as evidenced by consanguineous marriages of the parents; all are Japanese. These variants were designated as PK Tokyo, PK Nagasaki, PK Sapporo, PK Maebashi, PK Itabashi, PK Fukushima and PK Aizu, respectively. Low substrate affinity (high K0.5S for phosphoenolpyruvate) and thermal instability appear to play major roles in causing defective enzyme function, resulting in chronic haemolytic anaemia. Product inhibition of PK by ATP may also play an additional role in causing haemolysis in more than half the cases.

Invasive pulmonary aspergillosis (IPA) usually occurs in immunocompromised patients. However, rarely, this infection can occur in normal hosts. This review of the literature identified 13 cases of IPA associated with influenza, of which 12 had influenza A and the type of influenza was not mentioned in the other case. Reported here is a case of IPA, which was associated with influenza B, in a 63-year-old immunocompetent woman. Her lungs showed gross invasion and she was treated with itraconazole and amphotericin B. She required mechanical ventilation for about 5 months but recovered completely. This is the first reported case of IPA associated with influenza B.

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It is known that ABO blood group substances in human erythrocyte membranes are sphingoglycolipids, but recently several authors have reported that the glycoproteins of the erythrocyte membranes also have ABO blood group activities in addition to MN blood group activities and virus hemagglutination inhibitor activity. We solubilized blood group A erythrocyte membranes with lithium diiodosalicylate and separated the glycoprotein fraction by phenol extraction and ethanol precipitation. This fraction was apparently not contaminated with glycolipid, but it showed weak blood group A activity. The activity of the glycoprotein of the erythrocyte membranes was one-sixth of that of the lgycolipid fraction from the same amount of membranes. The glycoprotein components were purified by Sephadex G-200 gel filtration in SDS. The main component isolated, PAS 1, still showed blood A activity.