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Volume 26, Issue 2
Displaying 1-7 of 7 articles from this issue
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Gen MATSUMOTO, Michinori ICHIKAWA, Masashi URAYAMA, Shoichiro TSUKITA, ...1986 Volume 26 Issue 2 Pages 55-66
Published: March 25, 1986
Released on J-STAGE: May 25, 2009
JOURNAL FREE ACCESSWe have found that microtubule-depolymerizing reagents such as colchicine, podophyllotoxin and vinblastine reduce both sodium ionic and gating currents simultaneously, without affecting potassium currents appreciably. We have also found that calmodulin antagonist of W-7, trifluoperazine or chlorpromazine blocks the electrical excitability when applied intra-axonally. These indicate that subaxolemmal cytoskeleton of the squid giant axon plays a crucial role in maintenance and/or generation of the electrical excitability, and suggest that subaxolemmal cytoskeleton must be highly specialized.
We have demonstrated biochemically that subaxolemmal cytoskeleton is highly specialized and mainly composed of tubulin, actin, axolinin (a 260kd microtubule-associated protein) and a 255kd microfilament-associated protein. We have also found that the axolemma of the squid giant axon is specialized into two domains (microtubule- and microfilament-associated domains) by its underlying cytoskeletons.View full abstractDownload PDF (4179K) -
Current Status in Its Biochemical AspectHitoshi NAKAYAMA1986 Volume 26 Issue 2 Pages 67-72
Published: March 25, 1986
Released on J-STAGE: May 25, 2009
JOURNAL FREE ACCESSA sodium channel is well evaluated as a molecule which plays a key role in the nerve transmission since the excellent description by Hodgikin & Huxley on the basis of electrophysiological techniques in 1950s. Molecular entity of the channel, however, had not been thoroughly elucidated until the recent progress in biochemical approaches to purify it in a detergent-soluble form from eel electroplax, rat brain, and rat muscle. The purified channel protein from all three sources was reconstituted into phospholipid vesicles and shown to retain functional activity in a voltage dependent manner.
In addition, the relevance of the complete amino acid sequence of the eel channel protein can be viewed as inagurating a new phase of research on the molecular properties of ion channels in which the molecular architecture of their functional components is elucidated at ever finer resolution. Current status and questions to be resolved of the sodium channel molecule are reviewed in the biochemical aspect.View full abstractDownload PDF (1438K) -
Shin-ichi AIZAWA, Shigeru YAMAGUCHI1986 Volume 26 Issue 2 Pages 73-82
Published: March 25, 1986
Released on J-STAGE: May 25, 2009
JOURNAL FREE ACCESSFlagellar motor of bacteria is a rotary apparatus driven by protonmotive force. Flagellar basal body has been believed to be the major part of the motor, because it is the only structure detectable at the proximal end of the flagellum.
We developed a new method for the purification of the basal body and analysed the components by SDS-PAGE. The results showed the absence of mot gene products in the structure, suggesting that the functional part of the motor was lost during the purification of the basal body.
Three flagellar genes of Salmonella (flaQ, flaN and fla AII. 2) were found to be multifunctional, each giving rise to three distinct mutant phenotypes (Fla-, Mot- and Che-). The phenotypical diversity of these genes implys the participation of the gene products in flagellar assembly, motor rotation and control of the sense of rotation.
Genetic analysis of pseudorevertants from Mot- or Che- mutants of the multifunctional genes revealed the interaction among the three genes, suggesting that these gene products make a complex.
We present a new image of the motor, where a complex of the multifunctional gene products sits beneath the basal body as the stator of motor and has interaction with motA, B proteins and cheY, Z proteins.View full abstractDownload PDF (2292K) -
Keiji SHIKAMA1986 Volume 26 Issue 2 Pages 83-88
Published: March 25, 1986
Released on J-STAGE: May 25, 2009
JOURNAL FREE ACCESSThe stability properties of the iron (II)-dioxygen bond in Mb and Hb are of particular importance, since the oxygenated form is known to be oxidized easily to the ferric met-form, which cannot be oxygenated and is therefore physiologically inactive. Since the early work of the 1930's, it has been observed that the autoxidation rate increases with decreasing partial pressure of O2 and increases with increasing H+ concentration. Several proposals have therefore been made concerning the mechanism of this autoxidation reaction, and these can be classified into the following three types: (a) Oxidation, (b) Dissociation, and (c) Displacement.
These provide an interesting basis not only for future study, but also for a full understanding of general principles governing molecular oxygen enzymology including oxygenases and oxidases.View full abstractDownload PDF (317K) -
1986 Volume 26 Issue 2 Pages 88
Published: 1986
Released on J-STAGE: May 25, 2009
JOURNAL FREE ACCESSDownload PDF (37K) -
[in Japanese]1986 Volume 26 Issue 2 Pages 89-92
Published: March 25, 1986
Released on J-STAGE: May 25, 2009
JOURNAL FREE ACCESSDownload PDF (1316K) -
[in Japanese]1986 Volume 26 Issue 2 Pages 93-96
Published: March 25, 1986
Released on J-STAGE: May 25, 2009
JOURNAL FREE ACCESSDownload PDF (1637K)
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