journal article
LitStream Collection
Home
GLENNER, G. G.; KEISER, H. R.; BLADEN, H. A.; CUATRECASAS, P.; EANES, E. D.; RAM, J. S.; KANFER, J. N.; DELELLIS, R. A.
doi: 10.1177/16.10.633pmid: 5688086
Two morphologic components of human amyloid deposits, the periodic rod and the fibril, have been prepared free of cross-contamination. On tryptic digestion of guanidine-denatured material, peptide maps indicate these two components to have characteristic patterns with no detectable peptide fragments in common. Additional studies on ultrastructural morphology, physical characteristics and chemical composition reveal that the two components are clearly distinct entities with no evidence that one is a derivative of the other. The periodic rod, composed of stacked pentagonal unit structures or "doughnuts," is an antigenic globular glycoprotein deficient in tryptophan and methionine. The fibril, composed of laterally aggregated unit structures or filaments, is a poorly or nonantigenic fibrous glycoprotein of "pleated sheet" type containing both tryptophan and methionine. Congo red staining and birefringence, a dual characteristic of the fibrils and filaments, is dependent upon the physical integrity of these structures.
GROSSMAN, I. WILLIAM; HEITKAMP, DALE H.
doi: 10.1177/16.10.645pmid: 4235041
Magnesium-dependent adenosine triphosphatase (ATPase) activity of unfixed, isolated, intact skeletal muscle mitochondria, frozen-thawed mitochondria and digitonin-disrupted submitochondrial particles was localized ultrastructurally after incubation in a Wachstein-Meisel reaction medium and correlated with chemical ATPase activity. The reaction precipitate was localized within the matrix of intact and partially disrupted mitochondria and between membranous fragments in the submitochondrial particles. These findings are consistent with an ATPase activity residing within the headpieces of the elementary particles of mitochondrial cristae with deposition of reaction precipitate within the adjacent matrix.
BROLIN, SVEN E.; BERNE, CHRISTIAN; PETERSSON, BIRGER; LARSSON, ARNOLD
doi: 10.1177/16.10.654pmid: 4176940
The ability to hydrolyze various fructose phosphates was studied by microscopic histochemical techniques. The liver cells and the tubular cells of the kidney split fructose 1,6-diphosphate, fructose 1-phosphate and fructose 6-phosphate, whereas only the vessels of the islets and exocrine pancreatic parenchyma showed a positive reaction with these substrates. Whether the splitting of fructose 1,6-diphosphate takes place at position 1 or 6 cannot be revealed by estimation of liberated phosphate. In samples prepared by Lowry's microtechniques, liberated fructose 6-phosphate was determined fluorometrically by measuring reduced nicotinamide adenine dinucleotide phosphate formation in coupled phosphoglucoisomerase and glucose 6-phosphate dehydrogenase reactions. The activity of hexose diphosphatase (EC 3.1.3.11) in the liver of the NZO mouse was in the same range (0.5-1 MKH) as that found in other species. Samples of both pancreatic islets and acini showed only insignificant activities which could be attributed to the nonspecific phosphatases present in the vessels. The absence of hexose diphosphatase in the endocrine cells of the islets suggests that these cells cannot reutilize triosephosphates in the pentose phosphate shunt or for gluconeogenesis.
MASUOKA, DAVID; PLACIDI, GIAN-FRANCO
doi: 10.1177/16.10.659pmid: 5693926
A procedure for combining microautoradiography and the histochemical fluorescence method for aromatic monoamines on the same tissue section is described. The use of aqueous solutions is completely avoided, thus eliminating artifacts due to diffusion and dislocation of the labeled water-soluble drug and endogenous amines. The combination of these two techniques provides a means for obtaining data hitherto unavailable to correlate the site of binding and/or storage of water-soluble drugs with monoaminergic nerve cells and terminals.
Showing 1 to 9 of 9 Articles