scholarly journals A Histochemical Analysis of the Proteins in the Larval Fat Body of Sarcophaga Bullata

1966 ◽  
Vol 1 (1) ◽  
pp. 81-84
Author(s):  
KATHERINE A. BENSON ◽  
D. G. BENSON
Keyword(s):  
Nucleic Acids ◽  
Basic Protein ◽  
Fat Body ◽  
The Other ◽  
Acid Hydrolases ◽  
Histochemical Analysis ◽  
Fast Green ◽  
Sarcophaga Bullata ◽  
Control Procedures ◽  
Nuclear Histone

A comparison has been made between the basic proteins of the nucleus and the cytoplasm in the larval fat body cell of Sarcophaga bullata. Basic protein was found in four regions of the cell: in the nucleolus, in association with the DNA of the nucleus, as a diffuse reticulum extending throughout the cytoplasm, and as a complement of granules distributed throughout the cytoplasm. Of these four regions only the nucleolar basic protein was apparently unaffected by the blocking reactions of deamination and acetylation when stained with alkaline fast green. The proteins of the other regions were seen to be arginine-rich, but contained a sufficient amount of lysine to be slightly affected by control procedures. The cytoplasmic granular basic protein, lysosomal in nature, and the diffuse basic protein of the cytoplasm, RNA-associated, stained in exactly the same manner as did the nuclear histone with the three techniques used for histone demonstration and with the Sakaguchi reaction. Control procedures had no effect on the intensity of the Sakaguchi reaction in any region of the cell where arginine was demonstrable. It is suggested that the term histone be reserved for DNA-associated basic protein, and that some of the non-specificity of histone staining may be resolved by applying auxiliary methods for the demonstration of acid hydrolases or associated nucleic acids.

scholarly journals A MICROPHOTOMETRIC STUDY OF THE SYNTHESES OF DESOXYRIBONUCLEIC ACID AND NUCLEAR HISTONE

1955 ◽  
Vol 1 (1) ◽  
pp. 17-28 ◽  
Author(s):  
David P. Bloch ◽  
Gabriel C. Godman
Keyword(s):  
Cell Division ◽  
Nucleic Acids ◽  
Standard Error ◽  
Basic Protein ◽  
Desoxyribonucleic Acid ◽  
Fast Green ◽  
Nuclear Histone ◽  
Source Of Error ◽  
Formalin Fixed

1. The fast green stain of Alfert and Geschwind for nuclear basic protein is shown to obey the Beer-Lambert laws when used on purified histone. Interference from acid substances other than nucleic acids as a possible source of error is indicated. 2. Use of this technique after a modified Feulgen stain enables determination of relative amounts of desoxyribonucleic acid and histone in the same individual cells. 3. DNA and histone are shown to have the same distribution in formalin-fixed nuclei. 4. The syntheses of DNA and histone proceed simultaneously resulting in the doubling of both these substances prior to cell division. 5. The standard error for histone values is greater than that for DNA; however, the source of this variability is not known.

Electron Microscopy of Nucleic Acids

1974 ◽  
Vol 32 ◽  
pp. 302-303
Author(s):  
Norman Davidson
Keyword(s):  
Electron Microscopy ◽  
Nucleic Acids ◽  
Basic Protein ◽  
Molecular Biologist ◽  
Topological Properties ◽  
Protein Film ◽  
Polynucleotide Chain

The basic protein film technique for mounting nucleic acids for electron microscopy has proven to be a general and powerful tool for the working molecular biologist in characterizing different nucleic acids. It i s possible to measure molecular lengths of duplex and single-stranded DNAs and RNAs. In particular, it is thus possible to as certain whether or not the nucleic acids extracted from a particular source are or are not homogeneous in length. The topological properties of the polynucleotide chain (linear or circular, relaxed or supercoiled circles, interlocked circles, etc. ) can also be as certained.

Changes in protein spectra of bean seed during germination

1970 ◽  
Vol 48 (7) ◽  
pp. 1347-1350 ◽  
Author(s):  
Pei-Show Juo ◽  
G. Stotzky
Keyword(s):  
Acetic Acid ◽  
Phaseolus Vulgaris ◽  
Basic Protein ◽  
The Other ◽  
Globulin Fraction ◽  
Bean Seed ◽  
Basic Proteins ◽  
Number Of Components ◽  
Red Kidney Bean ◽  
Protein Spectra

Globulins, albumins, and basic proteins were extracted from seeds of red kidney bean (Phaseolus vulgaris), and their distribution was in a ratio of about 3:2:1, respectively. The globulin fraction constituted a major portion of the reserve proteins and was hydrolyzed rapidly during germination. More than 90% of the basic proteins, extractable with 0.05 N acetic acid, disappeared 12 days after germination. Although the decrease in total albumin was not as marked as with the other two fractions, a number of components of this fraction disappeared during the early stages of germination, but several new components were detected about 8 days after germination. The apparent synthesis of new globulin components during germination was also observed, but no synthesis of basic protein could be detected.

scholarly journals Metabolism of the nucleic acids of rumen bacteria by preruminant and ruminant lambs

1981 ◽  
Vol 45 (3) ◽  
pp. 517-527 ◽  
Author(s):  
M. A. Razzaque ◽  
J. H. Topps ◽  
R. N. B. Kay ◽  
J. M. Brockway
Keyword(s):  
Nucleic Acids ◽  
Bacterial Culture ◽  
Total Activity ◽  
Total Radioactivity ◽  
The Other ◽  
Nucleic Acid Content ◽  
Rumen Bacteria ◽  
Total Nucleic Acid ◽  
Purine Base ◽  
Close Relationship

1. A rumen bacterial culture containing specifically labelled nucleic acids was prepared using [8-14C]adenine.2. The labelled preparation was given in a liquid diet to two preruminant lambs and via a rumen tube to two ruminant lambs. The radioactivity excreted in exhaled gases, faeces and urine and that incorporated into tissues was determined.3 The preruminant lambs absorbed 58.3% of the total radioactivity measured after 24 h and the ruminant lambs 66.6% of the total activity measured after 48 h.4. Of the total radioactivity absorbed the preruminant lambs exhaled 38%, excreted 34% in urine and retained 29% in tissues. The corresponding values for the ruminant lambs were 12,41 and 47% respectively.5. There was a close relationship between total nucleic acid content and radioactivity per g of tissues of both preruminant and ruminant lambs.6. Of the radioactivity in the urine, the ruminant and one preruminant lamb excreted most in the fraction containing allantoin, while the other lamb excreted most activity in the uric acid fraction.7. The salvaging of the breakdown products of bacterial nucleic acids to make tissue nucleic acids appears to be an important synthesis in preruminant and ruminant lambs and of the likely precursors the purine base may be more important than the nucleoside.

scholarly journals On the Stereochemistry of the Interaction between Nucleic Acids and Basic Protein Side Chains.

1974 ◽  
Vol 28b ◽  
pp. 481-483 ◽  
Author(s):  
S. Furberg ◽  
J. Solbakk ◽  
Joseph R. Hlubucek ◽  
Bjarne Kimland ◽  
Curt R. Enzell ◽  
...  
Keyword(s):  
Nucleic Acids ◽  
Basic Protein ◽  
Side Chains

scholarly journals Secretion of β-N-acetylglucosaminidase isoenzymes by normal human fibroblasts

1978 ◽  
Vol 173 (2) ◽  
pp. 433-439 ◽  
Author(s):  
P Willcox
Keyword(s):  
Lysosomal Enzyme ◽  
Human Fibroblast ◽  
Lysosomal Enzymes ◽  
Culture Medium ◽  
Human Fibroblasts ◽  
The Other ◽  
Normal Human Fibroblast ◽  
Acid Hydrolases ◽  
Human Fibroblast Cultures ◽  
Normal Human

1. Secretion of the lysosomal enzyme beta-N-acetylglucosaminidase (EC 3.2.1.30) by normal human fibroblast cultures was linear with respect to time up to 96h. 2. Two forms of the A isoenzyme of beta-N-acetylglucosaminidase were found in the culture medium. One form was similar to the isoenzyme found in other extracellular fluids, such as plasma and tears, the other resembled the intracellular (lysosomal) enzyme. The presence of the two isoenzymes in the culture medium appears to reflect two distinct secretory processes. 3. It is suggested that plasma acid hydrolases may be destined for incorporation into lysosomes in a manner analogous to that described for the packaging of lysosomal enzymes by fibroblasts.

Some possibilities of representing microcirculation in human spleen

Biologia ◽  
2009 ◽  
Vol 64 (6) ◽  
Author(s):  
Paulína Gálfiová ◽  
Ivan Varga ◽  
Martin Kopáni ◽  
Peter Michalka ◽  
Jana Michalková ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Laser Scanning ◽  
Three Dimensional ◽  
Laser Scanning Confocal Microscopy ◽  
The Other ◽  
Corrosion Casts ◽  
Histochemical Analysis ◽  
Human Spleen ◽  
Scanning Confocal Microscopy ◽  
Scanning Electron

AbstractThe representation of microcirculation can be approached in several ways. One of the possibilities is to represent the endothelium (endothelial or sinus lining cells) and their basement membrane on the basis of detecting the known components and the expression of the surface antigenes by the methods of immuno-, enzyme- or lectino-histochemical analysis, or by staining or impregnation histological methods. The other possibility is the examination of samples by transmission and scanning electron microscopy. For three-dimensional demonstration corrosion casts techniques or laser scanning confocal microscopy can be used. In this paper we describe the survey of immuno-, enzyme- and lectino-histochemical characteristics of selected components of microcirculation and our own results of its demonstration in human spleen.

scholarly journals THE EFFECT OF POLY-L-LYSINE ON THE UPTAKE OF REOVIRUS DOUBLE-STRANDED RNA IN MACROPHAGES IN VITRO

1973 ◽  
Vol 57 (2) ◽  
pp. 484-498 ◽  
Author(s):  
Rolf Seljelid ◽  
Samuel C. Silverstein ◽  
Zanvil A. Cohn
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Surface ◽  
Nucleic Acids ◽  
Acid Hydrolases ◽  
Cell Compartment ◽  
Double Stranded Rna ◽  
Secondary Lysosomes ◽  
Toxic Concentrations ◽  
Vacuolar System

The effect of polycations on cultured mouse peitoneal macrophages has been examined. Polycations, at concentrations greater than 5 µg/ml, are toxic for macrophages) as measured by failure of the cells to exclude vital dyes. At toxic concentrations polycations bind in large amounts to nuclei and endoplasmic reticulum, while at nontoxic levels polycations bind selectively to the cell surface. Nontoxic concentrations of polycations stimulate binding of reovirus double-stranded (ds) RNA to the macrophages by forming polycation-dsRNA complexes either in the medium or at the cell surface. These complexes enter the cell in endocytic vacuoles and are concentrated in secondary lysosomes. Despite exposure to the acid hydrolases within this cell compartment, the dsRNA and the polycation (poly-L-lysine) are conserved in a macromolecular form within the vacuolar system. The mechanism(s) by which the uptake of infectious nucleic acids and the induction of interferon by dsRNA are stimulated by polycations are discussed.

The Synthesis of Nucleic Acids in Bacillus subtilis Infected with Phage PBS 1

1973 ◽  
Vol 51 (9) ◽  
pp. 1219-1224 ◽  
Author(s):  
B. K. Rima ◽  
I. Takahashi
Keyword(s):  
Bacillus Subtilis ◽  
Nucleic Acids ◽  
Dna Synthesis ◽  
Trichloroacetic Acid ◽  
Actinomycin D ◽  
The Other ◽  
Phage Dna ◽  
Infected Cells ◽  
Phage Growth ◽  
A New Species

Unlike other phage systems, the development of PBS 1 was found to be insensitive to rifamycin SV. The incorporation of 3H-uridine into trichloroacetic acid precipitable and alkali-labile material (RNA), in PBS-1-infected cells, was greatly reduced by rifamycin. Observations that RNA synthesized in the presence of rifamycin was hybridizable exclusively with the phage DNA and that actinomycin D inhibited the phage growth indicated that the synthesis of a new species of RNA was required for the development of PBS 1. The host DNA synthesis was reduced to a very low level 5 min after infection. The phage DNA synthesis was also apparently reduced markedly by rifamycin when determined with 3H-uridine as labelling material. On the other hand, rifamycin did not affect the incorporation of 3H-deoxycytidine into the phage DNA, suggesting that phage DNA synthesis was in fact insensitive to rifamycin. It is not clear how rifamycin inhibits the incorporation of 3H-uridine into nucleic acids in PBS-1-infected cells.

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