Staining of proteoglycans in mouse lung alveoli. I. Ultrastructural localization of anionic sites

1984 ◽  
Vol 16 (6) ◽  
pp. 657-669 ◽  
Author(s):  
T. H. M. S. M. Van Kuppevelt ◽  
J. G. W. Domen ◽  
F. P. M. Cremers ◽  
C. M. A. Kuyper
Keyword(s):  
Ultrastructural Localization ◽  
Mouse Lung ◽  
Anionic Sites

On the ultrastructural localization of cell surface sialyl residues versus anionic sites

1978 ◽  
Vol 36 (2) ◽  
pp. 294-295
Author(s):  
E. Skutelsky ◽  
S. Hoglund ◽  
B. Morein ◽  
E.A. Bayer
Keyword(s):  
Cell Surface ◽  
Ferric Hydroxide ◽  
Ultrastructural Localization ◽  
Anionic Sites ◽  
Successive Treatment ◽  
Coulombic Interaction ◽  
Thin Sections ◽  
Anionic Charge ◽  
Specific Localization

Membrane-associated sialic acids(SA) are considered to have an important role in a variety of cell sur ace interactions. Visualization of SA sites and their ultrastructural quantitative evaluation have heverally been based on the coulombic interaction between anionic sites of sialyl carboxyl groups with polycationic,electron dense markers, e.g. colloidal ferric hydroxide or cationized ferritin(CF). We have recently demonstrated an alternative method, whereby periodate-induced biotinylation (PIB) of unfixed cells can be used for specific localization of SA in thin sections by ferritin-conjugated avidin (FAv). It was further shown that PIB does not affect the surface anionic charge, since the latter is still available to CF-staining. In order to determine the role of anionic sites on the distribution and configuration of cell surface sialoglycoproteins and or sialoglycolipids, we have compared the topographic distribution of attached FAv or CF particles on normal and pathological blood cells,following successive treatment with sodium periodate and biotin hydrazide.

Ultrastructural localization of carbonyl reductase in mouse lung

1994 ◽  
Vol 26 (4) ◽  
pp. 311-316 ◽  
Author(s):  
Kazuya Matsuura ◽  
Yasuo Bunai ◽  
Isao Ohya ◽  
Akira Hara ◽  
Masayuki Nakanishi ◽  
...  
Keyword(s):  
Ultrastructural Localization ◽  
Carbonyl Reductase ◽  
Mouse Lung

ULTRASTRUCTURAL LOCALIZATION OF ANIONIC SITES IN THE RAT SKIN DEMONSTRATED WITH CATIONIC PROBES

1985 ◽  
Vol 12 (6) ◽  
pp. 472-478 ◽  
Author(s):  
Takashi Kazama ◽  
Itaru Kihara ◽  
Takashi Oite ◽  
Fujio Shimizu ◽  
Masaaki Ito ◽  
...  
Keyword(s):  
Ultrastructural Localization ◽  
Rat Skin ◽  
Anionic Sites

scholarly journals A simple two-step labeling procedure for ultrastructural localization of cell surface anionic sites.

1987 ◽  
Vol 35 (10) ◽  
pp. 1063-1067 ◽  
Author(s):  
E Skutelsky ◽  
E A Bayer
Keyword(s):  
Molecular Weight ◽  
Cell Surface ◽  
Blood Cells ◽  
Ultrastructural Localization ◽  
Low Ph ◽  
Low Molecular Weight ◽  
Cationized Ferritin ◽  
Anionic Sites ◽  
Secondary Interaction ◽  
Membrane Bound

We propose a new method for ultrastructural localization of cell surface anionic sites. The method consists of sequential interaction of aldehyde-fixed cells with a polycationic reagent, poly-L-lysine (PL), followed by secondary interaction with a negatively charged marker, ferritin. By use of PL of low molecular weight (4000) on aldehyde-pre-fixed red blood cells and macrophages, the reaction resulted in binding of ferritin particles to cell surface anionic sites with a density distribution resembling that of cationized ferritin (CF). The density of the attached ferritin molecules increased in direct correlation with the MW of PL used. The primary PL interaction can be carried out at low pH (less than 2), thus restricting the labeling mainly to membrane-bound sialyl residues.

Staining of proteoglycans in mouse lung alveoli. II. Characterization of the Cuprolinic Blue-positive, anionic sites

1984 ◽  
Vol 16 (6) ◽  
pp. 671-686 ◽  
Author(s):  
T. H. M. S. M. Van Kuppevelt ◽  
F. P. M. Cremers ◽  
J. G. W. Domen ◽  
C. M. A. Kuyper
Keyword(s):  
Mouse Lung ◽  
Anionic Sites ◽  
Cuprolinic Blue

Ultrastructural localization in the mouse lung of venom from the western diamondback (Crotalus atrox) rattlesnake

Toxicon ◽  
1984 ◽  
Vol 22 (6) ◽  
pp. 947-956 ◽  
Author(s):  
Rolf I. Schiff ◽  
Nicholas D. Cassai ◽  
Joseph F. Gennaro
Keyword(s):  
Ultrastructural Localization ◽  
Mouse Lung ◽  
Crotalus Atrox

Ultrastructural localization of specific nucleoprotein fractions

1978 ◽  
Vol 36 (2) ◽  
pp. 204-205
Author(s):  
G. L. Brown
Keyword(s):  
Gel Electrophoresis ◽  
Mouse Liver ◽  
Polyacrylamide Gel Electrophoresis ◽  
Ultrastructural Localization ◽  
Polyacrylamide Gel ◽  
Acid Extraction ◽  
Acid Solutions ◽  
Low Salt ◽  
Liver Nuclei ◽  
Phosphate Groups

Bismuth (Bi) stains nucleoproteins (NPs) by interacting with available amino and primary phosphate groups. These two staining mechanisms are distinguishable by glutaraldehyde crosslinking (Fig. 1,2).Isolated mouse liver nuclei, extracted with salt and acid solutions, fixed in either formaldehyde (form.) or gl utaraldehyde (glut.) and stained with Bi, were viewed to determine the effect of the extractions on Bi stainina. Solubilized NPs were analyzed by SDS-polyacrylamide gel electrophoresis.Extraction with 0.14 M salt does not change the Bi staining characteristics (Fig. 3). 0.34 M salt reduces nucleolar (Nu) staining but has no effect on interchromatinic (IC) staining (Fig. 4). Proteins responsible for Nu and glut.- insensitive IC staining are removed when nuclei are extracted with 0.6 M salt (Fig. 5, 6). Low salt and acid extraction prevents Bi-Nu staining but has no effect on IC staining (Fig. 7). When nuclei are extracted with 0.6 M salt followed by low salt and acid, all Bi-staining components are removed (Fig. 8).

Ultrastructural Localization of Acid Mucosubstance in Skeletal Muscle

1967 ◽  
Vol 25 ◽  
pp. 52-53 ◽  
Author(s):  
William J. Dougherty ◽  
Samuel S. Spicer
Keyword(s):  
Striated Muscle ◽  
Divalent Cations ◽  
Ultrastructural Localization ◽  
Major Elements ◽  
Frozen Sections ◽  
Thorium Dioxide ◽  
Iron Solution ◽  
Coupling System ◽  
Psoas Muscles ◽  
Formalin Fixed

In recent years, considerable attention has focused on the morphological nature of the excitation-contraction coupling system of striated muscle. Since the study of Porter and Palade, it has become evident that the sarcoplastic reticulum (SR) and transverse tubules constitute the major elements of this system. The problem still exists, however, of determining the mechamisms by which the signal to interdigitate is presented to the thick and thin myofilaments. This problem appears to center on the movement of Ca++ions between myofilaments and SR. Recently, Philpott and Goldstein reported acid mucosubstance associated with the SR of fish branchial muscle using the colloidal thorium dioxide technique, and suggested that this material may serve to bind or release divalent cations such as Ca++. In the present study, Hale's iron solution adapted to electron microscopy was applied to formalin-fixed myofibrils isolated from glycerol-extracted rabbit psoas muscles and to frozen sections of formalin-fixed rat psoas muscles.

Immunoenzymatic demonstration of the simultaneous presence of transferrin, hemopexin and albumin in a same hepatocyte and their ultrastructural localization

1978 ◽  
Vol 36 (2) ◽  
pp. 88-89
Author(s):  
M. Kraemer ◽  
J. Foucrier ◽  
J. Vassy ◽  
M.T. Chalumeau
Keyword(s):  
Plasma Proteins ◽  
Rat Hepatocytes ◽  
Ultrastructural Localization ◽  
Carrier Proteins ◽  
Normal Cells ◽  
Adult Rat ◽  
Adult Rat Hepatocytes ◽  
Monospecific Antisera ◽  
Different Levels

Some authors using immunofluorescent techniques had already suggested that some hepatocytes are able to synthetize several plasma proteins. In vitro studies on normal cells or on cells issued of murine hepatomas raise the same conclusion. These works could be indications of an hepatocyte functionnal non-specialization, meanwhile the authors never give direct topographic proofs suitable with this hypothesis.The use of immunoenzymatic techniques after obtention of monospecific antisera had seemed to us useful to bring forward a better knowledge of this problem. We have studied three carrier proteins (transferrin = Tf, hemopexin = Hx, albumin = Alb) operating at different levels in iron metabolism by demonstrating and localizing the adult rat hepatocytes involved in their synthesis.Immunological, histological and ultrastructural methods have been described in a previous work.

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