All issues
Volume 7 (1974)
- Issue 4 Pages 259-
- Issue 3 Pages 181-
- Issue 2 Pages 105-
- Issue 1 Pages 1-
Volume 7, Issue 3
Displaying 1-7 of 7 articles from this issue
- |<
- <
- 1
- >
- >|
-
KUNIAKI FUKUDA, HIDEYO SHINDO1974 Volume 7 Issue 3 Pages 181-183
Published: 1974
Released on J-STAGE: October 28, 2009
JOURNAL FREE ACCESSNon-specific esterase in the whole-body section of rat was demonstrated histochemically. A strong activity was seen in the liver, kidney cortex, pancreas, small intestine and Harderian gland and a weak activity in the hair follicles. The reaction was almost completely inhibited with 10-4M DFP except that in the hair follicles and Harderian gland, while not inhibited with 10-4M eserin. The usefulness of this method, “whole-body histochemistry”, was discussed.View full abstractDownload PDF (2245K) -
HISTOCHEMICAL DEMONSTRATION OF FRUCTOSE 1, 6-DIPHOSPHATASE IN RAT LIVER USING NITRO-BLUE TETRAZOLIUMHAJIME AOE1974 Volume 7 Issue 3 Pages 184-190
Published: 1974
Released on J-STAGE: October 28, 2009
JOURNAL FREE ACCESSThe activity of fructose 1, 6-diphosphatase (FDPase) in rat liver tissue was demonstrated histochemically using nitro-blue tetrazolium (nitro-BT) as a hydrogen accepting reagent. A fresh rat liver tissue was frozen by immersing into isopentane kept in an acetone and dry ice mixture. A slice of 8 micron thickness was fixed in a cold acetone (-20°C) for 30min, covered with a reaction mixture and incubated from 30 to 60min at 37°C. The incubation mixture is essentially an application of the assay system established for kinetic determination of FDPase activity at neutral pH; the formation of fructose 6-phosphate by FDPase reaction was coupled with a NADPH generating system using phosphoglucose isomerase (PGI) and glucose 6-phosphate dehydrogenase (G-6PDH) reaction.
The FDPase activity in liver tissue was demonstrated as a dark blue deposit of formazan in cytoplasm of parenchymal cells and was distributed relatively homogeneously in the lobule. The FDPase activity was inhibited by 5′-AMP, a speciffc inhibitor of FDPase.
The formazan deposit, which was demonstrated in rat liver by the present system, appeared to represent the localization of FDPase activity at neutral pH.View full abstractDownload PDF (4944K) -
HIROSHI KAITO1974 Volume 7 Issue 3 Pages 191-211
Published: 1974
Released on J-STAGE: October 28, 2009
JOURNAL FREE ACCESSThe histochemical and electron-microscopic investigations were performed on the functional aspects in the islet cells in starved rats, rabbits and guinea pigs.
Histologically, in starved animals, an atrophy of the B-cells was observed while the A-cells rather showed an increase in number.
Ultramicroscopically, the alterations in the exhausted condition induced by starvation, as indicated by the appearance of lipid droplets or ceroid substance, were observed not only in the B-cells but also in the A-cells.
On the contrary, in all starved animals, the tendency was demonstrated, electron-microscopically, that the B-cells appeared to be suppressed in their secretory function, whereas the A-cells appeared to be stimulated.
Enzyme-histochemical observations on the islets after fasting showed a decrease in the activity of Ac-Pase (rat and rabbit), G6Pase (rabbit and guinea pig), 5′Nase (rat) and IDPase, while an increase in the activity was demonstrated on ATPase, nonsp. Est., Al-Pase (rat) and many of the enzymes concerning glucose oxidation.
Enzyme activities in both the A-cells and the B-cells, determined histochemically, showed a synergistic alteration, and no antagonistic relationship was detected, although it was suggested under an electron microscope that, from the point of secretory function, the A-cells showed an antagonistic functional state to the B-cells.View full abstractDownload PDF (11580K) -
REIKO YOKOTA1974 Volume 7 Issue 3 Pages 212-216
Published: 1974
Released on J-STAGE: October 28, 2009
JOURNAL FREE ACCESSAn attempt was made for a histochemical demonstration of acid and alkaline phosphatases in the rat kidney and intestine, employing naphthyl phosphate as a substrate and tetrazotized benzidine as a new diazonium salt for coupling. By light microscopy, the azo dye deposit which was formed showed the site of these two kinds of enzymes to be reddish brown in color. Electron microscopy indicated that the enzyme reaction product yielded by alkaline phosphatases consists of electron opaque, fine grains on the duodenal epithelium of the rat. However, the reaction product by acid phosphatases tested in the rat kidney was so low in electron opacity that the lysosomes in the tissue did not show any appreciable increase in contrast.
These results show a usefulness of tetrazotized benzidine in the azo-coupling technique for light- and electron-microscopic localization of at least alkaline phosphatases.View full abstractDownload PDF (3299K) -
REIKO YOKOTA1974 Volume 7 Issue 3 Pages 217-230
Published: 1974
Released on J-STAGE: October 28, 2009
JOURNAL FREE ACCESSThe nonspecific esterase activity was investigated at the electron microscopic level, by means of azo dye technique applied to the duodenal, jejunal and ileal mucosae of living rats. After perfusion of a medium containing 1-naphthyl acetate and hexazonium pararosaniline into the lumen of the small intestine, the enzyme reaction product of electron opaque grains (50-100nm in diameter) was localized on the limiting membrane of microvilli of epithelial cells, and on the vesicles and the granular endoplasmic reticulum in the apical cytoplasm of epithelial cells. When the medium was perfused intravascularly, electron opaque grains were localized on the basal cell membrane and the basal lamina of epithelial cells as well as on the vesicles present in the basal cytoplasm of epithelial cells. Localizations of the esterase activity were essentially alike whether naphthyl propionate or butyrate was used as a substrate. The esterase activity in the duodenal and jejunal mucosae was higher than that in the ileal mucosa, judging from the results of inhibition test and reactivation test.View full abstractDownload PDF (14214K) -
OSAMU TAKEOKA1974 Volume 7 Issue 3 Pages 231-238
Published: 1974
Released on J-STAGE: October 28, 2009
JOURNAL FREE ACCESSWith an intraperitoneal injection of distilled water into the peritoneal cavity of rats, the peritoneal mast cells disappeared completely. Regenerating mast cells were studied two weeks after the injection. In these mast cells there was smooth transition in the structures of granules from a compact through a reticular granule to a granule with residual materials. This sequence was interpreted as a secretion process. This process was also observed in a few mast cells of control animals, but very active in the regenerating mast cells. Acid phosphatase activity of the mast cells in the control rats was observed in the Golgi apparatus and intergranular cytoplasmic matrix. No reaction was found in the granules except for a few granules of a few mast cells. A distinct positive reaction was observed in many granules of many regenerating mast cells. Acid phosphatase positive granules did not have a compact and homogeneous but a reticular structure in the regenerating mast cells as well as in a few mast cells of control animals. An intimate relationship observed between the transition of structures of granules and the intensities of their acid phosphatase reaction suggests that the acid phosphatase or enzymes activated simultaneously with the acid phosphatase play an important role in the degradation of the content of granules which would be secreted.View full abstractDownload PDF (13097K) -
FUMIE SASAKI1974 Volume 7 Issue 3 Pages 239-256
Published: 1974
Released on J-STAGE: October 28, 2009
JOURNAL FREE ACCESSThis paper presents the results of light and electron microscope histochemical studies of muscle fiber types in the anuran tadpole tail.
Two types of muscle fibers are distinguishable-the muscle fibers, (p.m. fibers) immediately below the layer of pigment cells of the skin; these are of smaller diameter and are abundant in sarcoplasm and mitochondria. The other type (i.m. fibers) is deep to the p.m. fibers; they are of relatively large diameter but contain less sarcoplasm and mitochondria.
Histochemical staining methods reveal stronger lactate dehydrogenase and succinic dehydrogenase activity in the p.m. fibers compared to the i.m. fibers. However, phosphorylase activity was more intensely visualized in the i.m. than the p.m. fibers. By these light and electron microscope histochemical observations, the small peripheral muscle fibers and the large inner muscle fibers have been tentatively classified as red and white muscle respectively.
The constant superficial distribution of the red muscle fiber in the tadpole tail is interesting and presents a unique condition for further study.View full abstractDownload PDF (31824K)
- |<
- <
- 1
- >
- >|