In the mixture of a solubilized membrane preparation and metal ion solution aggregates of particles 40-50Å in diameter or filamentous substances showing linear arrangement of particles were produced. When pH of the mixture was converted from 8 to 5 and incubated at 5°C for 12 hours, a number of vesicle membranes were produced.
By the same experimental procedure using pteridine granules of w^b mutant larvae incomplete formation of vesicle membranes was observed which may be due to the abnormality of their membrane protein.

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The intermediate and saturated forms of human hemoglobin-haptoglobin 1-1 complex were isolated by the use of preparative acrylamide gel electrophoresis.
The average molecular weights of the intermediate and saturated complexes, estimated by the sedimentation and diffusion studies, were 135, 000 and 169, 000, respectively. From these results, it was postulated that the intermediate and saturated complexes would be resulted from the combination of one molecule of haptoglobin 1-1 protein with an αβ-subunits and/or α₂β₂(2αβ) of hemoglobin A, respectively.

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Immunochemical characterization of the intermediate and saturated forms of human hemoglobin-haptoglobin 1-1 complex was performed by immunoprecipitation reaction using rabbit antisera against the α and β chains of normal human adult hemoglobin.
The intermediate and saturated complexes produced precipitation lines against antisera to either types of chain, indicating that these complexes contain both of the α- and β-chains of Hb A.
From these immunological studies and physico-chemical properties previously reported, it seems that the intermediate and saturated forms of Hb-Hp 1-1 complex would be Hp 1-1 bound with a αβ subunit and two αβ subunits (α₂β₂) of Hb A, respectively.

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The platelet-clumping substance in plasma collected from 200 hospitalized patients which included 34 healthy volunteers, was examined. The platelet-clumping substance was present in 4 out of 34 heparinized plasmas collected from healthy volunteers. It was markedly present in cases with an acute stage of thrombosis, bacterial infections, common colds, rheumatoid arthritis and malignant tumors (p<0.01). The platelet count in the cases of acute thrombosis and bacterial infections decreased significantly (p<0.05). In other miscellaneous diseases the appearance of the platelet-clumping substance and the decrease in the platelet count was not significant. The platelet-clumping substance was not detectable in serum and citrated, oxalated or EDTA-plasma, but the substance in heparinized plasma did not disappear after the addition of citrate, oxalate or EDTA to the plasma. It was stable for the storage at 4°C and was not dialyzable. These results suggest that the platelet-clumping substance in human plasma is similar to that previously detected in rabbit plasma and that it differs from ADP, thrombin, adrenaline and plasma cofactors of ADP.

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