Proceedings of the Japan Academy, Series B

Membrane Protein Transfer from Human Erythrocyte Ghosts to Liposomes Containing an Artificial Boundary Lipid

Ken-ichi SUZUKI, Yukihisa OKUMURA, Toshinori SATO, Junzo SUNAMOTO

1995 Volume 71 Issue 3 Pages 93-97
Published: 1995
Released on J-STAGE: October 13, 2006

DOIhttps://doi.org/10.2183/pjab.71.93

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When human erythrocyte ghost was exposed to a liposome that contains an artificial boundary lipid (1, 2-dimyristoylamido-1, 2-deoxyphosphatidylcholine, coded as D₁₄DPC), various kinds of membrane proteins and several lipids effectively transferred from the ghost to the liposome. The amount of proteins transferred increased with an increase in the D₁₄DPC content of the liposome. The SDS-PAGE analysis revealed the bands at 88kDa, 74kDa and 55kDa in the liposome after the exposure. No erythrocyte proteins larger than 88kDa were detected. Transfer of ACNE and band 3 was detected by using the enzymatic activity of AChE and a fluorescence probe specific to band 3. For the membrane protein transfer, an induction period was usually observed. The duration of the induction period was almost same for both of proteins, AChE and band 3. However, the transfer efficiency of band 3 was much less than that of AChE. Except the membrane proteins, a detectable amount of cholesterol also transferred from the ghost to the liposome. On the other hand, a significant amount of phospholipids simultaneously transferred from the liposome to the ghost.

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Cold Fusion Reactions Driven by “Latticequake”

Yoshiak ARATA, Yue-Chang ZHANG

1995 Volume 71 Issue 3 Pages 98-103
Published: 1995
Released on J-STAGE: October 13, 2006

DOIhttps://doi.org/10.2183/pjab.71.98

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The authors have proposed a new “Model” which can reasonably explain the existence of Cold Fusion Reaction and also verify the generation of tremendous excess energy in the DS-cathode, which is fifty thousand times higher than chemical reaction energy. The new model is named “Latticequake Model”. Cold fusion is caused by high energetic deuterium similar to “hot” fusion.

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Three-dimensional Structure of Abrin-a A-chain Having Ribosome Inactivating Activity

Tetsuya KOHNO, Toshiya SENDA, Hideki NARUMI, Shigenobu KIMURA, Yukio M ...

1995 Volume 71 Issue 3 Pages 104-107
Published: 1995
Released on J-STAGE: October 13, 2006

DOIhttps://doi.org/10.2183/pjab.71.104

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Three-dimensional structure of abrin-a A-chain has been solved by X-ray crystal structure analysis. The protein is a member of the Type II ribosome inactivating proteins (RIPs) which catalyze endohydrolysis of the N-glycosidic bond of a particular adenosine at position 4, 324 in 28S rRNA and thereby inhibit protein syntheses occurring on ribosome particles. It turned out that this enzyme had a similar three-dimensional structure to that of the A-chain of ricin, the crystal structure of which has been established before. The structure of abrin-a A-chain is composed of three domains, Domains 1, 2 and 3. The active site is located in the cleft which is surrounded by the surfaces of Domains 1, 2 and 3. The size of the cleft seems to be sufficient for recognizing RNA fragments including the GAGA tetraloop.

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DNA Recognition by a β-sheet

(2) Stereochemical Basis of DNA Bending by the β-sheets of MetJ and Arc Repressors

Masashi SUZUKI, Naoto YAGI

1995 Volume 71 Issue 3 Pages 108-113
Published: 1995
Released on J-STAGE: October 13, 2006

DOIhttps://doi.org/10.2183/pjab.71.108

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The stereochemical basis of DNA bending by a β-sheet is discussed in the light of crystal structures of MetJ and Arc repressors. The β-sheets of MetJ and Arc repressors bend the six basepair binding sites in the DNA to different directions. The β-sheet of MetJ compresses the major groove and thereby bends the DNA locally around the major groove, while that of ArcR widens the major groove at the centre and bends the DNA locally around the minor groove. Whether the major groove is compressed or widened seems to be dependent on the overall shape of the β-sheet, particularly the size of residues in some positions on the β-sheet. To close or open the major groove a pyrimidine-purine step at the centre of the binding site rolls to opposite directions.

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