Ultrastructural and biochemical studies on the isolation of nucleolar chromatin from Novikoff hepatoma cell nucleoli

Nucleolar chromatin of Novikoff hepatoma ascites cells contains an antigen (no-Ag1) detected with antinucleolar antibodies by the immunodiffusion technique. This antigen was distinguished from the previously reported nuclear chromatin antigen NAg-1 (19) by the findings that tumor nucleolar antibodies which formed immunoprecipitin bands with no-Ag1 did not do so with NAg-1 and that tumor cytosol, which contains NAg-1, formed immunoprecipitin bands with tumor chromatin antibodies but not with antibodies to tumor nucleoli. Tumor nucleolar chromatin contains both NAg-1 and no-Ag1, but only no-Ag1 formed bands with tumor nucleolar antibodies. no-Ag1 is a component of tumor nucleolar chromatin that was not soluble in 0.075 M NaCl - 0.025 M EDTA, pH 8, and only slightly soluble in 0.01 M Tris-HCl, pH 8. no-Ag1 was not found in liver nucleoli. Antibodies to liver nucleoli formed immunoprecipitin bands with liver nucleolar antigens but none were confluent with those formed between tumor nucleolar antibodies and antigens of tumor nucleolar chromatin. Absorption of the tumor nucleolar antibodies with whole tumor cells or whole liver pressate did not alter band formation with no-Ag1. Three antigens in liver nucleoli were not found in tumor nucleoli.

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Concanavalin a and Wheat Germ Agglutinin Receptors in the Ascitic Fluid of Rat Hepatomas

Tumori Journal ◽

10.1177/030089167906500102 ◽

1979 ◽

Vol 65 (1) ◽

pp. 9-18 ◽

Cited By ~ 2

Author(s):

Giovanni Neri ◽

Shelley Palmer Hayes ◽

Harilyn W. Smith ◽

Sylvia Capetillo ◽

Earl F. Walborg

Keyword(s):

Ascitic Fluid ◽

Concanavalin A ◽

Wheat Germ Agglutinin ◽

Wheat Germ ◽

Hepatoma Cell ◽

Hepatoma Cells ◽

Receptor Activity ◽

Con A ◽

Novikoff Hepatoma ◽

Lectin Receptors

The presence of glycopeptide lectin receptors in the ascitic fluid of rats bearing Novikoff or AS-30D hepatoma was investigated. Macrosialoglycopeptides, resistant to pronase digestion, were partially purified from the ascitic fluid of hepatoma-bearing rats by gel filtration on Sephadex G-50. A macrosialoglycopeptide fraction, isolated from the ascitic fluid of rats bearing the Novikoff hepatoma, possessed potent concanavalin A (Con A) receptor activity. This fraction possessed higher Con A receptor activity than did the comparable macrosialoglycopeptide fraction from the ascitic fluid of rats bearing the AS-30D hepatoma; this observation is in agreement with the Con A-induced agglutination properties of these 2 hepatoma cell lines and with the Con A receptor activities of the glycopeptides released from the surface of the hepatoma cells by papain digestion. Rat blood serum contained a comparable macrosialoglycopeptide fraction, which possessed weak Con A receptor activity. The macrosialoglycopeptide fractions from the ascitic fluid of hepatoma-bearing rats possessed wheat germ agglutinin receptor activity. However, this activity was also present in normal rat serum. These results suggest that glycopeptides present on the surface of Novikoff hepatoma cells are shed into the ascitic fluid and may be distinguished from components in normal serum by their Con A receptor activity.

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Ruthenium Red Staining of Human Hard Keratin Fibers

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100054005 ◽

1982 ◽

Vol 40 ◽

pp. 278-279

Author(s):

M. C. Buhrer ◽

R. A. Mathews

Keyword(s):

Human Hair ◽

Ruthenium Red ◽

Acid Mucopolysaccharides ◽

Biochemical Studies ◽

Keratin Fibers ◽

Ruthenium Red Staining ◽

Extracellular Materials

Ruthenium red has been used as a stain to demonstrate a variety of extracellular materials, especially acid mucopolysaccharides. It also reacts with certain intracellular and extracellular lipids. Since biochemical studies in our laboratory demonstrated the presence of a variety of monosaccharides in human hair ruthenium red staining procedures were adopted in order to evaluate the presence and morphological location of acid oligosaccharides in the keratinized aspect of hair.

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