All issues
Volume 16, Issue 2
Displaying 1-6 of 6 articles from this issue
- |<
- <
- 1
- >
- >|
-
SEIYA YAMAGUCHI, HISAO MATSUMOTO, MICHIYO HOSHIDE, KUNIKO AKITAKE1969 Volume 16 Issue 2 Pages 53-56
Published: September 25, 1969
Released on J-STAGE: August 11, 2009
JOURNAL FREE ACCESSDownload PDF (2144K) -
K. NODA1969 Volume 16 Issue 2 Pages 57-67
Published: September 25, 1969
Released on J-STAGE: August 11, 2009
JOURNAL FREE ACCESSIn the isolated frog sartorius muscles, it has been determined by washout experiments of radioactive Ca, Na or P that the maintenance of physicochemical integrity, especially in lipid components, is required for making membrane depolarization but the physicochemical firmness is probably presumed by the difference in turnover rates of ions on the charged sites. The release of these ions was considered as the physical process like an ion exchange. The effects of lipase and depolarization were comparatively investigated from the viewpoint of site occupation of ions. 1. Although 45Ca dissociation from the muscles was, similar in grade and different in time course, enhanced not only in Ca free or high K Ringer but in Ca free lipase Ringer or high K lipase Ringer to cause membrane depolarization, 22Na efflux which was observed at the same time demonstrated a difference between the first two and the other two. The difference is probably due to the difference in grade of exchange or turnover of Na ions at the sites which were originally occupied by Ca ions and were participating probably in constructing lipid components. The difference in turnover rate may be equivalent to the difference in physical tightness of macromolecules. 2. The membrane depolarization resulted in the increase in 45Ca dissociation, however, the enhancement did not cause parallelly the change in 22Na movement in the muscles depolarized by Ca free or high K Ringer and in those by Ca free lipase or high K lipase Ringer probably because of the difference in location of Ca sites affected. The difference in turnover rate of Na ions at the membrane sites sequentially occupied is not dependent upon the grade of decalcification from the membrane but upon the place of Ca ions which have been substitutably occupied by Na ions. 3. When no external Ca ions were present the release of 32P incorporated was marked. This type of release, on the contrary, became difficult to occur when lipid component of the membrane was simultaneously disintegrated. As far as the movement of 32P from the muscle surface is concerned membrane depolarization is not always presumed by lipolytically releasing 32P. Even under depolarizing conditions, when lipolysis was accompanied, newly accumulated Na ions were immobilized and releaseable P was hardly mobilized.View full abstractDownload PDF (3753K) -
PART 4 : THE MUSCLES OF THE UPPER LIMBSADATO SATO1969 Volume 16 Issue 2 Pages 69-81
Published: September 25, 1969
Released on J-STAGE: August 11, 2009
JOURNAL FREE ACCESSDownload PDF (1066K) -
SHIGERU YAMAMOTO, HIDEFUMI KABUTA, YOH NAKAGAWA1969 Volume 16 Issue 2 Pages 83-89
Published: September 25, 1969
Released on J-STAGE: August 11, 2009
JOURNAL FREE ACCESSPlaque formation by herpes simplex virus was reduced by treatment of cells with protamine sulfate before virus inoculation. Protamine composing amino acids or trypsin digested protamine had no plaque reducing effect. Protamine could not inactivate the virus by itself. More virus particles remained unadsorbed and intact in the inoculum to protamine-pretreated cell cultures than that in controls. Protamine solution once mixed with cells lost the plaque reducing effect. These results strongly suggested that protamine molecules bind to cell surface (receptor) to prevent virus particles from attaching to receptors.View full abstractDownload PDF (639K) -
HIDEFUMI KABUTA, SHIGERU YAMAMOTO, MIZUKO TANIKAWA, YOH NAKAGAWA1969 Volume 16 Issue 2 Pages 91-99
Published: September 25, 1969
Released on J-STAGE: August 11, 2009
JOURNAL FREE ACCESSA comparison was made for HF and M strains of herpes simplex virus for their thermosensitivity in various conditions. The infectivity of herpes viruses were preserved well by 10% bovine serum and 1% skim milk in PBS at 45°C for 10 minutes. The titers of HF and M strains showed pretty well preservations by PBS, MLE and 10% glycerin in PBS. The thermostabilizing effects of 10% DMSO, 1 M MgCl2, 1 M Na2SO4 in PBS and distilled water were fairly inferior. The thermostability of M strain under the various conditions was greater than HF strain. The range of optimal pH for high thermostability was more comprehensive in M strain as compared to HF strain.View full abstractDownload PDF (838K) -
HITOMI NAKAGAWA1969 Volume 16 Issue 2 Pages 101-112
Published: September 25, 1969
Released on J-STAGE: August 11, 2009
JOURNAL FREE ACCESS1. Rats fed on thiamine-deficient diet showed a slight increase in body weight for the first two weeks but the body weight decreased thereafter. 2. Wet weight of the liver tissue from the thiamine-deficient rats increased slightly during the first 18 days, but after they remained constant. 3. The most of the thiamine which was found in cytoplasm of the liver cell was decreased rapidly as the result of deprivation of thiamine in the diet. 4. In polysomal pattern which was analyzed by sucrose gradient centrifugation, heavy polysomes tended to increase after 7 days of thiamine deficiency and incorporation of 3H-orotic acid also increased in the polymer portion which were larger than trimer. After 25 to 31 days of thiamine deficiency, heavy polysomes decreased and light polysomes increased markedly. The Ratio of polysomes which is heavier than hexamer to the total polysome showed a transitory increase after 7 days of thiamine deficiency but decreased thereafter. 5. Specific activity of 3H-orotic acid incorporated into polysomal RNA in vivo and that of 14 C-leucine incorporated into polysome in vitro also showed a transitory increase after 7 days of deficiency and then decreased thereafter. Both recovered rapidly by the administration of thiamine.View full abstractDownload PDF (2286K)
- |<
- <
- 1
- >
- >|