scholarly journals THE EFFECTIVENESS OF OUR COLLOIDAL IRON METHOD IN THE ELECTRON-HISTOCHEMICAL DEMONSTRATION OF SULFHYDRYL AND DISULPHIDE WITH PARTICULAR REFERENCE TO PANCREATIC ZYMOGEN GRANULES

1975 ◽  
Vol 8 (4) ◽  
pp. 372-379
Author(s):  
NOBUO IHARA ◽  
RYUICHI SANO ◽  
JUNKO TOKI ◽  
RYUEI MAEDA
Keyword(s):  
Histochemical Demonstration ◽  
Zymogen Granules ◽  
Colloidal Iron

scholarly journals HISTOCHEMICAL AND ULTRASTRUCTURAL DEMONSTRATION OF γ-GLUTAMYL TRANSPEPTIDASE ACTIVITY

1969 ◽  
Vol 17 (8) ◽  
pp. 517-526 ◽  
Author(s):  
ALEXANDER M. RUTENBURG ◽  
HWAKYU KIM ◽  
JEROME W. FISCHBEIN ◽  
JACOB S. HANKER ◽  
HANNAH L. WASSERKRUG ◽  
...  
Keyword(s):  
Azo Dye ◽  
Histochemical Demonstration ◽  
Zymogen Granules ◽  
Optimum Conditions ◽  
Histochemical Reaction ◽  
Copper Chelate ◽  
Electron Microscopic ◽  
Apical Portion ◽  
Glutamyl Transpeptidase ◽  
Electron Microscopic Localization

A simultaneous coupling azo dye method for the histochemical demonstration of γ-glutamyl transpeptidase activity using the new substrate γ-glutamyl-4-methoxy-2-naphthylamide has been described. The method appears superior to previously reported methods for γ-glutamyl transpeptidase activity and can easily be modified for the electron microscopic localization of the enzyme by bridging osmium to the copper chelate of the azo dye via thiocarbohydrazide. The optimum conditions for the histochemical reaction were developed and the distribution of enzymatic activity in the tissues of the rat is described for light microscopy and with rat pancreas for electron microscopy. The electron-opaque deposits were seen in the endoplasmic reticulum in the vicinity of the zymogen granules in the apical portion of the acinar cell.

Localization of pancreatic enzymes in ultrathin frozen sections stained with metal labeled antibody

1978 ◽  
Vol 36 (2) ◽  
pp. 90-91
Author(s):  
Kenjiro Yasuda
Keyword(s):  
Fluorescent Antibody ◽  
Pancreatic Enzymes ◽  
Tissue Preparation ◽  
Zymogen Granules ◽  
Frozen Sections ◽  
En Bloc ◽  
Antibody Method ◽  
Ultrathin Frozen Sections ◽  
Fluorescent Antibody Method

Localization of amylase,chymotrypsinogen and trypsinogen in pancreas was demonstrated by Yasuda and Coons (1966), by using fluorescent antibody method. These enzymes were naturally found in the zymogen granules. Among them, amylase showed a diffuse localization around the nucleus, in addition to the zymogen granules. Using ferritin antibody method, scattered ferritin granules were also found around the Golgi area (Yasuda et al.,1967). The recent advance in the tissue preparation enables the antigen to be localized in the ultrathin frozen sections, by applying the labeled antibodies onto the sections instead of staining the tissue en bloc.The present study deals with the comparison of the localization of amylase and lipase demonstrated by applying the bismuth-labeled, peroxidase-labeled and ferritin-labeled antibody methods on the ultrathin frozen sections of pancreas, and on the blocks of the same tissue.

The Fine Structure of Glycocalyx in Human Spermatozoa. A High Resolution Cytochemical Study

1973 ◽  
Vol 31 ◽  
pp. 640-641
Author(s):  
P. Hernández-Jáuregui ◽  
A. Sosa ◽  
A. González Angulo
Keyword(s):  
Negative Charge ◽  
Iron Hydroxide ◽  
Human Spermatozoa ◽  
Surface Coat ◽  
Cell Surfaces ◽  
Colloidal Iron ◽  
Cytochemical Study ◽  
Specific Permeability ◽  
Extracellular Glycoprotein ◽  
Mammalian Spermatozoa

Glycocalyx is the name given by Bennett to the extracellular glycoprotein coat present in some cell surfaces. It appears to play an important role in cell properties such as antigenicity, cell adhesivity, specific permeability, and ATP ase activity. In the sperm this coat can be directly related to such important phenomena as capacitation and fertilization. The presence of glycocalyx in invertebrate spermatozoa has already been demonstrated. Recently Yanagimachi et al. has determined the negative charges on sperm surfaces of mammalian spermatozoa including man, using colloidal iron hydroxide. No mention was made however of the outer surface coat as composed of substances other than those confering a negative charge. The purpose of this work was therefore to determine the presence of a glycocalyx in human spermatozoa using alcian blue and lanthanum staining.

The diagnosis of metabolic storage disease in skin biopsies (a light-, electronmicroscopic, and analytical study)

1978 ◽  
Vol 36 (2) ◽  
pp. 648-649
Author(s):  
W. Jurecka ◽  
W. Gebhart ◽  
H. Lassmann
Keyword(s):  
Storage Disease ◽  
Hunter Syndrome ◽  
Histochemical Demonstration ◽  
Sweat Glands ◽  
Type I ◽  
Storage Material ◽  
Scheie Syndrome ◽  
Storage Products ◽  
Skin Biopsies ◽  
Type V

Diagnosis of metabolic storage disease can be established by the determination of enzymes or storage material in blood, urine, or several tissues or by clinical parameters. Identification of the accumulated storage products is possible by biochemical analysis of isolated material, by histochemical demonstration in sections, or by ultrastructural demonstration of typical inclusion bodies. In order to determine the significance of such inclusions in human skin biopsies several types of metabolic storage disease were investigated. The following results were obtained.In MPS type I (Pfaundler-Hurler-Syndrome), type II (Hunter-Syndrome), and type V (Ullrich-Scheie-Syndrome) mainly “empty” vacuoles were found in skin fibroblasts, in Schwann cells, keratinocytes and macrophages (Dorfmann and Matalon 1972). In addition, prominent vacuolisation was found in eccrine sweat glands. The storage material could be preserved in part by fixation with cetylpyridiniumchloride and was also present within fibroblasts grown in tissue culture.

Resolution of Channels in the Exine by Translocation of Colloidal Iron

1971 ◽  
Vol 29 ◽  
pp. 352-353
Author(s):  
John R. Rowley
Keyword(s):  
Phosphate Buffer ◽  
Pollen Development ◽  
Osmium Tetroxide ◽  
Pollen Grains ◽  
Deionized Water ◽  
Colloidal Iron ◽  
Fixed Material ◽  
Epilobium Angustifolium ◽  
Untreated Material ◽  
Microspore Mitosis

The morphology of the exine of many pollen grains, at the time of flowering, is such that one can suppose that transport of substances through the exine occurred during pollen development. Holes or channels, microscopic to submicroscopic, are described for a large number of grains. An inner part of the exine of Epilobium angustifolium L. and E. montanum L., which may be referred to as the endexine, has irregularly shaped channels early in pollen development although by microspore mitosis there is no indication of such channeling in chemically fixed material. The nucleus in microspores used in the experiment reported here was in prophase of microspore mitosis and the endexine, while lamellated in untreated grains, did not contain irregularly shaped channels. Untreated material from the same part of the inflorescence as iron treated stamens was examined following fixation with 0.1M glutaraldehyde in cacodylate-HCl buffer at pH 6.9 (315 milliosmoles) for 24 hrs, 4% formaldehyde in phosphate buffer at pH 7.2 (1,300 milliosmoles) for 12 hrs, 1% glutaraldehyde mixed with 0.1% osmium tetroxide for 20 min, osmium tetroxide in deionized water for 2 hrs and 1% glutaraldehyde mixed with 4% formaldehyde in 0.1M cacodylate-HCl buffer at pH 6.9 for two hrs.

A complex network of “snake-like tubules” revealed by the NADPase cytochemical reaction in the acinar cell of pancreas

1984 ◽  
Vol 42 ◽  
pp. 666-667
Author(s):  
A.R. Beaudoin ◽  
G. Grondin ◽  
A. Lord ◽  
M. Pelletier
Keyword(s):  
Acinar Cell ◽  
Lead Acetate ◽  
Ultrastructural Localization ◽  
Sodium Acetate Buffer ◽  
Zymogen Granules ◽  
Sprague Dawley ◽  
Dense Bodies ◽  
Sprague Dawley Rats ◽  
Cytochemical Reaction ◽  
Cellular Organelles

We have recently described the ultrastructural localization of NADPase activity in the exocrine pancreas of rat. The enzyme was found in the intermediate saccules of the Golgi apparatus, in dense bodies and lysosomes but was absent from zymogen granules. A very intense reaction was noticed in a peculiar structure which was termed “Snake-Like Tubule” (SLT). The purposes of the present study were firstly to delineate SLT distribution in the acinar cell and secondly to define any possible relationship or association with other cellular organelles.NADPase cytochemical reaction was performed on the pancreas of adult Sprague Dawley rats. Small lobules were excised and fixed for 50 min, at 4°C, in 2% glutaraldehyde buffered with 0.1M cacodylate at pH 7.2. Lobules were rinsed several times with the same buffer containing 570 sucrose and cut with a Mcllwayn tissue chopper. Sections were washed several times with buffer and incubated for 2 hr at 37°C in the following medium: 4mM NADPH; 40mM sodium acetate buffer, pH 5.0; 4mM lead acetate and 5% sucrose.

Mitochondrial Oxidation of p-N, N-Dimethylamino-β-Phenethylamine (DAPA)

1975 ◽  
Vol 33 ◽  
pp. 458-459
Author(s):  
W. Allen Shannon ◽  
Hannah L. Wasserkrug ◽  
andArnold M. Seligman
Keyword(s):  
Guinea Pig ◽  
Oxidase Activity ◽  
Amine Oxidase ◽  
Histochemical Demonstration ◽  
Guinea Pig Heart ◽  
Pig Kidney ◽  
Cytoplasmic Vacuoles ◽  
Liver And Kidney ◽  
Mitochondrial Oxidation ◽  
Amine Oxidase Activity

The synthesis of a new substrate, p-N,N-dimethylamino-β-phenethylamine (DAPA)3 (Fig. 1) (1,2), and the testing of it as a possible substrate for tissue amine oxidase activity have resulted in the ultracytochemical localization of enzyme oxidase activity referred to as DAPA oxidase (DAPAO). DAPA was designed with the goal of providing an amine that would yield on oxidation a stronger reducing aldehyde than does tryptamine in the histochemical demonstration of monoamine oxidase (MAO) with tetrazolium salts.Ultracytochemical preparations of guinea pig heart, liver and kidney and rat heart and liver were studied. Guinea pig kidney, known to exhibit high levels of MAO, appeared the most reactive of the tissues studied. DAPAO reaction product appears primarily in mitochondrial outer compartments and cristae (Figs. 2-4). Reaction product is also localized in endoplasmic reticulum, cytoplasmic vacuoles and nuclear envelopes (Figs. 2 and 3) and in the sarcoplasmic reticulum of heart.

Reticuloendothelial Function and Blood Coagulation in Rats

1969 ◽  
Vol 22 (03) ◽  
pp. 508-512
Author(s):  
L Pechet ◽  
Giselle S. Pechet ◽  
R. A MacDonald
Keyword(s):  
Blood Coagulation ◽  
Free Carbon ◽  
Colloidal Iron ◽  
Intravascular Coagulation ◽  
India Ink ◽  
Carbon Clearance

SummaryIntravascular coagulation and its possible effect on carbon clearance was studied in rats following the injection of commercial india ink containing shellac; a shellac-free carbon preparation; gelatin; heat denatured albumin; colloidal iron; and heparin. No relationship was found between activation of coagulation and RES function as measured by clearance of intravenously injected carbon.

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