bluuebunny/crossref_metadata_2025_split huggingface dataset:
Submicroscopic Organization of Retinal Cones of the Rabbit
Authors: De Robertis Eduardo , Lasansky Arnaldo 
Published: May 2004

The fine structure of the cone cell of the rabbit is described and compared wtih that of the rod. The cone outer segment consists of a pile of flattened sacs with two membranes 30 A thick and a regular clear space in between of about 30 A. The membrane of the rod sacs is slightly thicker (∼40 A) and the clear space is less regular and frequently absent in the deeper regions. The distance between sacs is from 85 to 95 A in the cone and from 110 to 120 A in the rod, and the total repeating period is about 190 A and 210 A, respectively. These results are discussed in relation to the concentration of solids in both photoreceptors.
A connecting cilium was observed in the cone cell and compared with that previously described in rods (4). This finding suggests that morphogenetically the cone may also result of the differentiation of a primitive cilium (5).
The inner segment of the cone shows a distal portion with large concentration of elongated mitochondria and a proximal one with a large Golgi complex in the axis surrounded by components of the endoplasmic reticulum. It is concluded that both photoreceptors have a similar general plan of submicroscopic organization, with some minor difference in fine structure probably related to their specific chemical composition and function.
The Influence of Age, Sex, Pregnancy, Starvation, and Other Factors on the Cytoplasmic Ribonucleoproteins of Rat Liver
Authors: Petermann Mary L. , Hamilton Mary G. 
Published: May 2004

Rat liver was homogenized in 0.88 M sucrose. The DNA and total RNA were determined, and the homogenate was fractionated by differential centrifugation. The pellets obtained between 30 minutes at 20,000 g and 180 minutes at 105,000 g were analyzed for RNA and nitrogen. The ribonucleoproteins were determined in the analytical ultracentrifuge. The non-pellet RNA was calculated by difference. The results are reported as amounts per 6.7 x 10-9 mg. of DNA.
In young, growing male rats the amounts of microsomal protein and ribonucleoprotein B (83S) increased with age. Non-pregnant adult females showed less non-pellet RNA and much more ribonucleoprotein C (63S) than did adult males.
During pregnancy both of these cell constituents reverted to levels characteristic for male animals. Starvation for 5 days resulted in a reduction in the mass of liver tissue, the non-pellet RNA, the microsomal protein, and ribonucleoproteins B and C. During recovery from starvation the return of the liver to normal paralleled the rate at which body weight was restored. Treatment with cortisone, 25 mg. per rat per day for 5 days, caused an increase in microsomal protein and a decrease in ribonucleoprotein B. Treatment with 6-mercapto-purine, 50 mg. per kilo per day for 5 days, caused little change in liver composition in either males or females.
A Cytological Analysis of the Antimetabolite Activity of 5-Hydroxyuracil in Vicia faba Roots
Authors: Schreiber Richard W. , Duncan Robert E. 
Published: May 2004

The effects of 5-hydroxyuracil (5-HU) (isobarbituric acid) upon cell elongation, mitosis, and DNA synthesis were studied in Vicia faba roots.
5-HU had no consistent effect upon root elongation. It blocked DNA synthesis (analyzed by photometric measurements of Feulgen dye in nuclei) during the first 6 hours of treatment; the block spontaneously disappeared by the 12th hour of treatment.
Uracil and thymine had no effect upon this block of synthesis. Both thymidine and uridine reversed the block in 6 and 9 hours respectively.
In all cases blockage of DNA synthesis was followed by inhibition of mitosis (determined by changes in the percentage of cells in mitosis) and resumption of DNA synthesis was followed by resumption of mitosis. Inhibition indices calculated from the mitotic data indicated a competitive relationship between 5-HU and thymidine and 5-HU and uridine.
5-HU is considered to block DNA synthesis by competing with thymidine for sites on enzymes involved in the synthesis. It is suggested that uridine reverses the block in synthesis by undergoing a conversion to thymidine.
PHOSPHOLIPID METABOLISM IN INTACT AND MODIFIED ERYTHROCYTE MEMBRANES
Authors: Redman Colvin M. 
Published: May 2004

Erythrocyte membranes incorporated labeled phosphate from γ-adenosine triphosphate (AT32P) into phosphatidic acid and the polyphosphoinositides. Inositol-3H and palmitate-14C were also incorporated into the phospholipids but α-glycerophosphate-32P was not. The incorporation of γ-AT32P into phospholipids was increased when the erythrocyte ghosts were incubated in hypotonic media which lysed the cells. Lysis had little or no effect on the incorporation of inositol-3H and palmitate-14C into the phospholipids.
If erythrocyte membranes were prepared in 1 mM ethylenediaminetetraacetate (EDTA), instead of 1 mM MgCl2, then the tonicity of the incubating medium did not influence the incorporation of γ-AT32P into the phospholipids. Erythrocyte ghosts, prepared by lysis in water, EDTA, or 1 mM calcium, lead, mercury, zinc, or cadmium, failed to reconstitute when placed in isotonic medium, inasmuch as they did not retain potassium against a chemical gradient. Ghosts prepared by lysis in 1 mM magnesium, barium, or strontium could be reconstituted. Ghosts which failed to reconstitute incorporated more labeled phosphate from γ-AT32P into the phospholipids than did intact or reconstituted ghosts. The larger incorporation of labeled phosphate by leaky ghosts was not due to a greater entrance of γ-AT32P into those cells.
Primaquine phosphate and digitonin, at concentrations which are known to cause cells to form smaller vesicles or to lyse cells by removing cholesterol, did not increase the incorporation of labeled phosphate into the phospholipids.
It is suggested that the increased metabolism of phospholipids may be involved in a membrane repair mechanism.
Collagen Formation by Fibroblasts of the Chick Embryo Dermis
Authors: Porter Keith R. , Pappas George D. 
Published: May 2004

This investigation has sought to determine the relation between collagen fiber and fibroblast during fibrogenesis. Toward this end the surfaces of chick fibroblasts grown under in vitro conditions have been examined with the electron microscope after fixation in OsO4. Supplementary information has been obtained from thin sections of fibroblasts fixed in situ during phases of fiber production.
The evidence provided by these studies and by various conditions of the experiments indicates that the unit fibrils of collagen form in close association with the cell surface. They were never observed within the cell. When these unit fibrils form in bundles it appears as though templates of some nature, possibly coinciding with stress fibers within the cell cortex, influence the polymerization of the fibrils out of material available at the cell surface. From here the fibrils and bundles of them are shed into the intercellular spaces and there grow to limited diameters by accretion of materials from the general milieu.
Heteromorphic Change of Adult Fibroblasts by Ribonucleoproteins
Authors: Benitez Helena H. , Murray Margaret R. , Chargaff Erwin 
Published: May 2004

Cultures of subcutaneous areolar fibroblasts from adult rats, when confronted in vitro with microsomes from rat liver or kidney, are changed heteromorphically so as to resemble cultures of nervous tissue. Similar effects follow exposure to the deoxycholate-insoluble fraction of microsomes, and to purified RNA from rat liver or from yeast. An equivalent ribonucleoside mixture has no heteromorphic effect.
The degree of heteromorphosis can be related quantitatively to the amount of RNA administered, up to a maximum of 150 γ per slide, above which toxicity intervenes. Ribonuclease destroys in considerable degree the effectiveness of the active agents.
Heteromorphosis cannot be induced in this adult tissue by a short exposure (1 to 3 hours) followed by removal to normal medium. A 24 hour exposure to microsome suspensions, however, is followed by partial change lasting for at least several days. Results are most clear cut when cultures of the explant type are maintained continuously in contact with the RNA-containing agents; nevertheless, cell suspensions exposed for 2 to 3 days to heteromorphic agents in suitable concentration appear to be permanently changed.
Interspecies experiments between rat and mouse indicate that rat fibroblasts are more labile than mouse, and/or rat microsomes are more potent as agents of heteromorphosis. Mouse liver microsomes have no morphogenetic effect on homologous fibroblasts, but exert a slight action on rat fibroblasts. Rat microsomes have a growth-stimulating effect, but no heteromorphic action, on mouse fibroblasts.
Purified protein from snake venom, which is highly active as a growth factor for avian nervous tissue, is growth-stimulating to rat fibroblasts but has no heteromorphic action on this material.
The Incorporation of Leucine-C14 into Microsomal Particles and other Subcellular Components of the Pea Epicotyl
Authors: Ts'o Paul O. P. , Sato Clifford S. 
Published: May 2004

Incorporation of leucine-C14 into subcellular fractions of the apical section of pea seedlings has been studied as a function of the length of incubation. The specific activity of the microsomes was higher than that of the supernatant for short but not for long incubations, in agreement with observations on other systems. In this developing tissue the nuclei and especially the mitochondria appear to incorporate amino acid very rapidly. An insoluble fraction of the microsome pellet, which is presumably a liponucleoprotein complex, was found to possess, after 1 hour of incubation, a specific activity much greater than that of the purified microsomal particles or the supernatant fraction.
Ninety-eight per cent of the leucine-C14 in the purified microsomal particles has been shown to possess bound amino groups, presumably in peptide linkages, by the DNP-end group method. These particles liberate but little peptide or protein of very high specific activity when they are destroyed by removal of Mg or by hydrolysis of RNA.
Microsomal particles were fractionated into an RNA fraction and five protein fractions by means of density gradient centrifugation. By this method 95 per cent of the RNA can be separated from 90 per cent of the protein of the particle. Furthermore, the RNA fraction has been shown to contain very little protein of high specific activity. A particular protein fraction which contains the remaining 5 per cent of the RNA, possessed after 1 hour of incubation a specific activity 2 to 9 times higher than the protein of the other fractions.
Cytological Evidence that Both RNA and DNA May Form a Complex with the Same Protein
Authors: Littau Virginia C. 
Published: May 2004

Deoxyribonucleic acid can be added back to protein sites from which the original nucleic acid, ribo- or deoxyribo-, is removed. If sections of frozen-substituted ovarian follicle cells of a leafhopper are first extracted by hot trichloracetic acid to remove nucleic acids and then immersed in a solution of a commerical preparation of deoxyribonucleic acid, the nucleic acid becomes attached to nuclear and cytoplasmic sites and can be rendered visible by the Feulgen reaction. The addition occurs in certain other tissues as well.
The results are discussed in relation to biochemical and other cytochemical investigations of the nucleoprotein complex.
Factors Influencing the Histochemical Demonstration of Coenzyme-Dependent Dehydrogenases and Diaphorases
Authors: Cascarano Joseph , Zweifach Benjamin W. 
Published: May 2004

Procedures for the histochemical demonstration of DPN and TPN diaphorases have been presented by other workers. These techniques rely on the coenzyme-dependent dehydrogenases present in the tissue slice to generate the substrate required by the diaphorases. In vitro studies were carried out on kidney and adrenal tissue of the rat, using NT (neotetrazolium) and INT (2-p-iodophenyl-3-p-nitrophenyl-5-phenyl tetrazolium chloride) with various substrates of DPN-dependent dehydrogenases. The solutions used for study contained alcohol and alcohol dehydrogenase, glutamate and malate, malate, glutamate, ß-hydroxybutyrate, or DPNH. It has been possible to demonstrate (1) that histological distribution of dehydrogenases may differ from that of the flavoprotein oxidizing reduced coenzyme I; (2) characteristic patterns of distribution of particular dehydrogenases in the tissue proper; (3) different levels of dehydrogenase in kidney and adrenal; and (4) differences in dehydrogenase distribution in the kidneys of man and rat.
The evidence presented clearly indicates the limitations inherent in the accepted procedures for the demonstration of DPN and TPN diaphorases. The possible application of the tetrazolium salts to the study of particular coenzyme-dependent dehydrogenases and the pitfalls which might occur are also discussed.
A PARACRYSTALLINE INCLUSION IN NEUROSPORA CRASSA
Authors: Wood David D. , Luck David J. L. 
Published: May 2004

A paracrystal indistinguishable from the one which occurs in the mitochondrial mutant abnormal-1 can be induced in wild-type Neurospora crassa after growth in either ethidium or euflavine. This paracrystal has been isolated and partially characterized. It appears to be composed of a single polypeptide (mol wt 68,000) which can be reversibly crystallized and dissociated by changes in the pH and ionic strength. When aggregated, the polypeptide forms oligomers which are arranged end-to-end into fibers.
During the characterization of the polypeptide, it was found that the polypeptide's electrophoretic and immunological properties could be used as assays. Using these methods it was found that the polypeptide normally accumulates in a soluble form in the cytoplasm of wild-type Neurospora at the end of the log-phase of growth.
CYTOPLASMIC SYNTHESIS OF NUCLEAR PROTEINS
Authors: Wu Roy S. , Warner Jonathan R. 
Published: May 2004

The synthesis of cytoplasmic and nuclear proteins has been studied in HeLa cells by examining the amount of radioactive protein appearing in the various subcellular fractions after labeling for brief periods. Due to the rapid equilibration of the amino acid pool, the total radioactivity in cytoplasmic protein increases linearly. The radioactivity observed in the cytoplasm is the sum of two components, the nascent proteins on the ribosomes and the completed proteins. At very short labeling times the specific activity of newly formed proteins found in the soluble supernatant fraction (completed protein) increases as the square of time, whereas the specific activity of the ribosomal fraction (nascent protein) reaches a plateau after 100 sec. The kinetics of accumulation of radioactive protein in the nucleus and the nucleolus is very similar to that of completed cytoplasmic protein, which suggests that the proteins are of similar origin. The rate of release and migration of proteins from the ribosomes into the nucleus requires less time than the synthesis of a polypeptide, which is about 80 sec. The uptake of label into nucleolar proteins is as rapid as the uptake of label into proteins of the soluble fraction of the cytoplasm, while nuclear proteins, including histones, tend to be labeled more slowly. The same results are obtained if protein synthesis is slowed with low concentrations of cycloheximide.
The kinetics of incorporation of amino acids into various fractions of the cell indicates that the nucleus and the nucleolus contain few if any growing polypeptide chains, and thus do not synthesize their own proteins.
Spermiogenesis in Lumbricus herculeus
Authors: Gatenby J. Brontë , Dalton A. J. 
Published: May 2004

Small pieces of the sperm sacs of Lumbricus herculeus were fixed for 4 hours in chrome-osmium, embedded in methacrylate, sectioned with a Porter-Blum microtome, and studied with a R.C.A. EMU-2C electron microscope.
Each spermatid of a group developing synchronously is attached by a cytoplasmic strand to a common nutrient protoplasmic mass. This mass contains mitochondria and yolk bodies but is anucleate.
The proximal centriole, that is, the centriole nearer the nucleus, is at first associated with a small peg which becomes firmly attached to the nuclear membrane. Later these two bodies become separated during the development of the middle-piece which is differentiated in the usual manner from a nebenkern formed by the fusion of 6 or 7 mitochondria.
The acrosome develops in relation to the dictyosome (Golgi body), itself composed of 8 or more individual flattened sacs and situated in the cytoplasm opposite the point of attachment of the spermatid to the nutrient mass. Soon after its formation, the acrosome becomes incorporated into a cytoplasmic appendage or acrosome carrier. The carrier moves from its original position, along the lateral border of the elongating nucleus, to the distal margin of the nucleus where the acrosome is deposited. No evidence was found of a centriole located at the point of junction between nucleus and acrosome as suggested by earlier workers.
Dynamics of Spindle Formation and Its Inhibition by Chemicals
Authors: Taylor Edwin W. 
Published: May 2004

The formation of the mitotic spindle of the newt cell in tissue culture has been studied, using polarized light. The rate of formation was measured and it was shown that the spindle increased in length at a constant rate until the maximum was attained. During metaphase the spindle shortened to about 50 to 60 per cent of its original length, reaching a minimum just before anaphase. No birefringence was detected in late anaphase in the spindle region after the chromosome masses had separated.
The effects of certain compounds which are believed to inhibit protein synthesis were investigated. Chloramphenicol added in early prophase prevented the formation of a spindle of normal length. The possible relation of chloramphenicol to the synthesis of spindle proteins is discussed.
Differents aspects du fer dans l'organisme
Authors: Bessis Marcel , Breton-Gorius Janine 
Published: May 2004

Des cellules réticulaires remplies de molécules de ferritine et d'hémosidérine se trouvent au centre "d'ilots érythroblastiques."
Dans la zone de contact entre la cellule réticulaire chargée de ferritine et les érythroblastes, on voit des invaginations et des petites vacuoles au bord desquelles adhérent des molécules de ferritine. Il est postulé que la ferritine passe de la cellule réticulaire centrale dans les érythroblastes par ce mécanisme, apparenté à la pinocytose (rhophéocytose).
Dans tous les érythroblastes normaux, il existe du fer sous forme de ferritine. Celle-ci peut se trouver à l'état dispersé ou agglomérée en amas. Lorsque ces amas sont assez gros, ils sont visibles au microscope optique: ce sont les granules des sidéroblastes.
On trouve du fer dans les mitochondries, mais rarement à l'état normal. Il est soit sous forme de granules ferritiniques soit sous forme de micelles ferrugineuses.
Dans les thalassémies et d'autres maladies s'accompagnant d'un trouble de l'hémoglobinogénèse, on trouve, en grande quantité, du fer visible au microscope électronique, dans les érythroblastes. Il s'y trouve sous forme de ferritine, en amas ou dispersé. Il existe parfois en grande quantité dans les mitochondries soit sous forme de ferritine, soit sous forme de micelles ferrugineuses.
Il semble que soit objectivé ainsi le trouble de la synthèse de l'hémoglobine: le fer inutilisé s'accumule dans des érythroblastes hypochromes.
Il est probable qu'à l'etat normal, le fer est métabolisé dans les mitochondries. Dans le thalassémies et les anémies hypochromes hypersidérémiques, il semble souvent bloqué dans ces organites.
Fine Structure of Cellular Inclusions in Measles Virus Infections
Authors: Kallman Frances , Adams John M. , Williams Robley C. , Imagawa David T. 
Published: May 2004

Cells which are infected with measles virus have been known for some time to contain inclusion material that is distinguishable from normal cellular components by application of traditional staining methods and observation in the light microscope. The fine structure of the inclusion material contained in HeLa cells infected with Edmonston strain of measles virus has been examined in the electron microscope. Two steps have been found necessary in this study: (1) the recognition by phase-contrast microscopy of the living cell of bodies that are defined as inclusion material when the cells are classically stained; and (2) the recognition in the electron microscope of inclusion-body material that had previously been identified in the living cell.
The fine structure of the nuclear and cytoplasmic inclusion material in osmium-treated cells was found to consist mainly of randomly arrayed filaments of low electron density. Dense, highly ordered arrays of filaments were found near the center of the nuclear inclusions, sometimes as a two-dimensional, nearly orthogonal arrangement. If the size of the measles virus is taken to be around 100 mµ in diameter, the strands seen in the inclusions cannot be fully formed virus.
Electron Microscopy of Neurospora crassa Mycelia
Authors: Shatkin A. J. , Tatum E. L. 
Published: May 2004

The fine structure of vegetative mycelia of the filamentous Ascomycete, Neurospora crassa, has been investigated by the standard techniques of electron microscopy. Addition of uranyl nitrate to the methacrylate-embedding medium minimized disruption of the specimens—an accident often observed in the preparation of microbial material.
This report describes the presence of a chitinous polysaccharide wall containing fine fibrils embedded in a homogeneous matrix. A sinuate plasma membrane lies adjacent to the inner wall surface. This membrane is often closely associated with the endoplasmic reticulum of the cytoplasm. Numerous mitochondria of the classical type, and dense particles of 10 mµ diameter occur throughout the cytoplasm. The nuclear region is surrounded by a double membrane with pore openings. Associated with the nuclear envelope is a dense area, the nucleolus.
The significance of these observations and their relationship to other forms is discussed.
PROPERTIES OF PHYSARUM MYOSIN PURIFIED BY A POTASSIUM IODIDE PROCEDURE
Authors: Nachmias V. T. 
Published: May 2004

Myosin has been purified free of actin from Physarum actomyosin by a two step adaptation of the classical potassium iodide method for depolymerizing actin. On 12% sodium dodecyl sulfate (SDS) gels, the single major slowly moving protein band present in the calcium activated adenosine triphosphatase peak (90% pure) is associated with two fast moving bands of molecular weights of approximately 17,000 and 21,000 daltons, respectively. Densitometry shows the molar ratio of heavy chains to the 21,000 and 17,000 dalton chains on the gels to be 1:2:1.
The highly purified myosin forms filaments up to 2.5 µm long in the presence of 5 mM magnesium and 0.05 M KCl. Calcium ions were not required for the formation of long filaments from this highly purified myosin.
At low ionic strength (0.05 M KCl) the magnesium ATPase of the highly purified myosin is activated four- to tenfold by muscle actin. The extent of activation is a function of the actin concentration and levels off at high levels of actin. In 0.1 mM calcium salts the ATPase activity is approximately 60% of that in 1 mM EGTA.
In summary, Physarum myosin is similar to a number of muscle myosins as well as to platelet and fibroblast myosin, which all possess light chains of two different molecular weights associated with the heavy chains. Under ionic conditions close to those in vivo, highly purified Physarum myosin aggregates into long filaments.