concanavalin-a and thiocarbohydrazide
concanavalin-a has been researched along with thiocarbohydrazide* in 4 studies
Other Studies
4 other study(ies) available for concanavalin-a and thiocarbohydrazide
Article | Year |
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Ultrastructural cytochemistry of aortic microfibrils in the Arctic lamprey, Lampetra japonica.
In the ventral aorta of lamprey, microfibrils are major components of the extracellular matrix. With special reference to these microfibrils, we have cytochemically examined the lamprey ventral aorta, utilizing the tannic acid (pH 7.0)-uranyl acetate (TA-UA) method, elastase en bloc digestion, Thiéry's periodic acid-thiocarbohydrazide-silver proteinate (PA-TCH-SP) method, and ferritin- or horseradish peroxidase-labeled concanavalin A (Con A) methods. The lamprey microfibrils were strongly stained with PA-TCH-SP and both Con A methods, but did not show TA-UA staining nor elastase sensitivity. These cytochemical properties of lamprey microfibrils are identical with those of mammalian elastin-associated microfibrils. On the other hand, in spite of extensive examination, TA-UA positive and elastase-sensitive extracellular components were not found, so that lamprey ventral aorta does not appear to contain elastin. These results indicate that lamprey aortic connective tissue contains microfibrils as elastic components, but deposition of amorphous elastin does not occur. Topics: Actin Cytoskeleton; Animals; Aorta; Carbohydrate Metabolism; Concanavalin A; Cytoskeleton; Elastin; Ferritins; Fishes; Glycols; Histocytochemistry; Horseradish Peroxidase; Hydrazines; Lampreys; Microscopy, Electron; Periodic Acid; Silver Proteins | 1989 |
Ultrastructural visualization of carbohydrates in oxytalan fibers in monkey periodontal ligaments.
Fullmer's oxytalan fibers appear to be special connective tissue fibers belonging to elastic system fibers. We have ultrastructurally examined carbohydrates in oxytalan fibers in monkey periodontal ligaments after glutaraldehyde fixation and ethylenediaminetetraacetic acid (EDTA) decalcification using: Thiéry's periodic acid-thiocarbohydrazide-silver proteinate (PA-TCH-SP) method for thin-section staining of vicinal glycol-containing complex carbohydrates, and the concanavalin A-ferritin (Con A-ferritin) and Con A-horseradish peroxidase (Con-A-HRP) en bloc staining methods specific for alpha-D-mannosyl and alpha-D-glucosyl groups. PA-TCH-SP stained collagen fibrils weakly to moderately and stained oxytalan fibers moderately. Con A-ferritin and Con A-HRP stained collagen fibrils weakly or moderately and stained oxytalan fibers intensely within the superficial region of specimen blocks. The penetration of staining reagents was improved by prior saponin treatment and/or chondroitinase ABC digestion. Thus, these studies demonstrate that PA-TCH-SP and Con A staining of carbohydrates is very useful in identifying oxytalan fibers at the ultrastructural level and that more carbohydrate components are present in oxytalan fibers than in collagen fibrils. Topics: Animals; Carbohydrates; Chondroitin Lyases; Concanavalin A; Connective Tissue; Contractile Proteins; Extracellular Matrix Proteins; Ferritins; Histocytochemistry; Horseradish Peroxidase; Hydrazines; Macaca; Male; Microscopy, Electron; Periodic Acid; Periodontal Ligament; RNA Splicing Factors; Saponins; Silver Proteins; Staining and Labeling | 1985 |
The carbohydrates of secretory granules and the glycocalyx in developing mucoid cells.
Complex carbohydrates in secretory granules and at the apical cell surface of mouse gastric mucoid cells were studied during embryogenesis and in the early postnatal period by various cytochemical methods; the periodic acid-thiocarbohydrazide-silver proteinate (PA-TCH-SP) and tannic acid-uranyl acetate (TA-UA) procedures made neutral mucosubstances (NMS) visible, whereas the hexose residues of glycoconjugates were identified using WGA-, RCA II- and ConA-ferritin. The glycocalyx was stained with ruthenium red (RR). During differentiation of the embryonic mucoid cells the number of secretory granules increased in parallel to the increase in their carbohydrate component. NMS-stainable parts in secretory granules also had binding sites for the conjugates RCA II- and WGA-ferritin, but the binding of ConA could not be identified. The increasing quantity of NMS in secretory granules was correlated with the increased amount of PA-TCH-SP and TA-UA positive substances in the apical glycocalyx only in 14- and 18-day-old embryos. The observed uniform affinity for RR and lectin conjugates in all analysed developmental stages remains to be explained. Topics: Animals; Animals, Newborn; Cell Membrane; Concanavalin A; Cytoplasmic Granules; Embryo, Mammalian; Ferritins; Gastric Mucosa; Glycosaminoglycans; Histocytochemistry; Horseradish Peroxidase; Hydrazines; Hydrolyzable Tannins; Lectins; Mice; Organometallic Compounds; Periodic Acid; Plant Lectins; Ruthenium Red; Silver Proteins; Staining and Labeling; Uranium; Wheat Germ Agglutinins | 1985 |
Ultrastructural cytochemistry of carbohydrates in microfibrils associated with the amorphous elastin in the monkey aorta.
Two distinct ultrastructural components of elastic fibers can be identified--namely, the amorphous elastin and the microfibrils. We have examined the tunica adventitia of monkey aortas to demonstrate differential localization of carbohydrates in elastic fibers and collagen fibrils using Thiéry's periodic acid-thiocarbohydrazide-silver proteinate (PA-TCH-SP) staining of thin sections for vicinal-glycol-containing complex carbohydrates, en bloc concanavalin A (Con A) staining specific for alpha-D-mannosyl and alpha-D-glucosyl groups, and en bloc wheat germ agglutinin (WGA) staining specific for N-acetyl-D-glucosamine, N-acetylneuraminic acid, and N-acetyl-D-galactosamine. The PA-TCH-SP method moderately stained microfibrils and weakly stained collagen fibrils, but did not stain the amorphous elastin. Both Con A and WGA staining methods strongly stained microfibrils and moderately stained collagen fibrils, whereas the amorphous elastin lacked staining. Thus PA-TCH-SP, Con A, and WGA staining methods allow differential ultrastructural localization of carbohydrates in elastic fibers and collagen fibrils in monkey aortic adventitia and demonstrate the presence of more carbohydrate components in microfibrils than in collagen fibrils, whereas amorphous elastin lacks carbohydrate staining. Topics: Animals; Aorta; Carbohydrate Metabolism; Concanavalin A; Elastic Tissue; Ferritins; Histocytochemistry; Horseradish Peroxidase; Hydrazines; Macaca; Male; Periodic Acid; Silver Proteins; Staining and Labeling | 1985 |