scholarly journals STUDIES OF THE TRANSMISSIBLE AGENT OF THE ROUS CHICKEN SARCOMA I

1940 ◽  
Vol 72 (6) ◽  
pp. 697-705 ◽  
Author(s):  
David Shemin ◽  
E. E. Sproul ◽  
James W. Jobling
Keyword(s):  
Basic Protein ◽  
Active Agent ◽  
Basic Proteins ◽  
Rous Sarcoma

The viscosity of Rous sarcoma extracts can be reduced with a polysaccharide enzyme isolated from pneumococcus or testis without destruction of the active agent and thus more concentrated active filtrates can be obtained. The active agent can be precipitated with basic proteins. The basic protein can be separated from the components originally coming from the tumor filtrate by electrophoresis.

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 Proteolytic and peroxidatic reactions of commercial horseradish peroxidase with myelin basic protein

1978 ◽  
Vol 169 (3) ◽  
pp. 567-575 ◽  
Author(s):  
Wendy Cammer ◽  
Lesley Z. Bieler ◽  
William T. Norton
Keyword(s):  
Horseradish Peroxidase ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Protein A ◽  
Low Molecular Weight ◽  
Basic Proteins ◽  
Molecular Weights ◽  
Low Concentrations ◽  
High Concentrations ◽  
A Minor

Degradation of myelin basic protein during incubations with high concentrations of horseradish peroxidase has been demonstrated [Johnson & Cammer (1977) J. Histochem. Cytochem.25, 329–336]. Possible mechanisms for the interaction of the basic protein with peroxidase were investigated in the present study. Because the peroxidase samples previously observed to degrade basic protein were mixtures of isoenzymes, commercial preparations of the separated isoenzymes were tested, and all three degraded basic protein, but to various extents. Three other basic proteins, P2 protein from peripheral nerve myelin, lysozyme and cytochrome c, were not degraded by horseradish peroxidase under the same conditions. Inhibitor studies suggested a minor peroxidatic component in the reaction. Therefore the peroxidatic reaction with basic protein was studied by using low concentrations of peroxidase along with H2O2. Horseradish peroxidase plus H2O2 caused the destruction of basic protein, a reaction inhibited by cyanide, azide, ferrocyanide, tyrosine, di-iodotyrosine and catalase. Lactoperoxidase plus H2O2 and myoglobin plus H2O2 were also effective in destroying the myelin basic protein. Low concentrations of horseradish peroxidase plus H2O2 were not active against other basic proteins, but did destroy casein and fibrinogen. Although high concentrations of peroxidase alone degraded basic protein to low-molecular-weight products, suggesting the operation of a proteolytic enzyme contaminant in the absence of H2O2, incubations with catalytic concentrations of peroxidase in the presence of H2O2 converted basic protein into products with high molecular weights. Our data suggest a mechanism for the latter, peroxidatic, reaction where polymers would form by linking the tyrosine side chains in basic-protein molecules. These data show that the myelin basic protein is unusually susceptible to peroxidatic reactions.

Cytoplasmic DNA and basic protein synthesis in Megalobatrachus davidianus oocytes

Development ◽  
1971 ◽  
Vol 26 (2) ◽  
pp. 271-283
Author(s):  
Y. C. Kong ◽  
I. F. Lau ◽  
W. L. Lam ◽  
C. M. Choy
Keyword(s):  
Protein Synthesis ◽  
Dna Synthesis ◽  
Dose Response ◽  
Dna Content ◽  
Active Site ◽  
Basic Protein ◽  
Basic Proteins ◽  
Biochemical Event ◽  
Cytoplasmic Dna

Mature Megalobatrachus oocytes contain 43 µg DNA per oocyte, as compared with 250 pg DNA in a hepatocyte of the same animal. Megalobatrachus oocytes respond to CdR treatment by an increased incorporation of [3H]lysine into basic proteins associated with ooplasmic particles, with an optimal CdR concentration at 2 mM. The nucleolus is the most active site of [3H]lysine incorporation. It is suggested that CdR-stimulated basic protein synthesis is a common biochemical event during amphibian oogenesis. The dose response to CdR treatment may be a function of the c-DNA content or c-DNA synthesis potential in the ooplasm.

Two-dimensional gel electrophoresis of human brain proteins. V. Non-equilibrium gel electrophoresis, with detection of a myelin basic protein mutation--MBL-Duarte.

1982 ◽  
Vol 28 (4) ◽  
pp. 813-818 ◽  
Author(s):  
D E Comings ◽  
A Pekkula-Flagan
Keyword(s):  
Human Brain ◽  
Myelin Basic Protein ◽  
Gel Electrophoresis ◽  
Basic Protein ◽  
Myelin Proteins ◽  
Two Dimensional Gel Electrophoresis ◽  
Brain Proteins ◽  
Basic Proteins ◽  
A Charge ◽  
Non Equilibrium

Abstract To examine the basic human brain proteins, we subjected 9 mmol/L urea extracts to non-equilibrium gel electrophoresis. The pattern observed differs distinctly from that with equilibrium gel electrophoresis. With this technique, the myelin proteins (myelin basic protein, proteolipids, and basic Wolfgram proteins) and many other unindentified major basic proteins can be demonstrated. The myelin basic proteins occur as two major polypeptides of different charge and slightly different molecular mass, indicating the action of at least two genes. The proteolipid proteins occur as a long series of charge isomers, suggesting multiple genes or extensive post-transcriptional modification. In one patient with schizophrenia, a charge-change mutation of the larger myelin basic protein (MBL) was observed and is termed "MBL-Duarte."

scholarly journals Myelin basic proteins in myelin subfractions from normal and quaking mice

1979 ◽  
Vol 183 (1) ◽  
pp. 159-162
Author(s):  
G E Fagg ◽  
T V Waehneldt
Keyword(s):  
Distribution Pattern ◽  
Basic Protein ◽  
Littermate Control ◽  
Basic Proteins ◽  
Myelin Subfractions ◽  
And Control ◽  
Quaking Mice

The relative proportions of four myelin basic proteins (preL, L, preS,S) were determined in myelin subfractions prepared from the forebrains of quaking and littermate control mice. The distribution pattern of each protein was similar in both mutant and control fractions. The S component was the only basic protein present in low amounts in myelin from the mutant.

scholarly journals Ethanol Extraction of Basic Proteins From Ejaculated Human Spermatozoa

1979 ◽  
Vol 32 (5) ◽  
pp. 443 ◽  
Author(s):  
Peter French
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Banding Pattern ◽  
Gel Electrophoresis ◽  
Basic Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Ethanol Extraction ◽  
Basic Proteins ◽  
Unconventional Method

A method for the extraction of basic proteins from human ejaculated spermatozoa has been developed It relies on the previously unreported observation that such basic protein is soluble in a solution containing 60% (v/v) ethanol. This unconventional method yields a high percentage of arginine-rich basic protein which is then able to be characterized on the basis of its amino acid composition. This method also allows comparisons to be made between single ejaculates by the banding pattern each displays when subjected to polyacrylamide gel electrophoresis.

scholarly journals Phosphate groups modifying myelin basic proteins are metabolically labile; methyl groups are stable.

1983 ◽  
Vol 97 (2) ◽  
pp. 438-446 ◽  
Author(s):  
K C DesJardins ◽  
P Morell
Keyword(s):  
Half Life ◽  
Time Course ◽  
Basic Protein ◽  
Turnover Time ◽  
Methyl Groups ◽  
Peptide Backbone ◽  
Radioactive Label ◽  
Basic Proteins ◽  
Precursor Pool ◽  
Phosphate Groups

Young and adult rats received intracranial injections of [33P]orthophosphoric acid. The time course of the appearance and decay of the radioactive label on basic proteins in isolated myelin was followed for 1 mo. Incorporation was maximal by 1 h, followed by a decay phase with a half-life of approximately 2 wk. However, radioactivity in the acid-soluble precursor pool (which always constituted at least half of the total radioactivity) decayed with a similar half-life, suggesting that the true turnover time of basic protein phosphates might be masked by continued exchange with a long-lived radioactive precursor pool. Calculations based on the rate of incorporation were made to more closely determine the true turnover time; it was found that most of the phosphate groups of basic protein turned over in a matter of minutes. Incorporation was independent of the rate of myelin synthesis but was proportional to the amount of myelin present. Experiments in which myelin was subfractionated to yield fractions differing in degree of compaction suggested that even the basic protein phosphate groups of primarily compacted myelin participated in this rapid exchange. Similar studies were carried out on the metabolism of radioactive amino acids incorporated into the peptide backbone of myelin basic proteins. The metabolism of the methyl groups of methylarginines also was monitored using [methyl-3H]methionine as a precursor. In contrast to the basic protein phosphate groups, both the peptide backbone and the modifying methyl groups had a metabolic half-life of months, which cannot be accounted for by reutilization from a pool of soluble precursor. The demonstration that the phosphate groups of myelin basic protein turn over rapidly suggests that, in contrast to the static morphological picture, basic proteins may be readily accessible to cytoplasm in vivo.

scholarly journals Investigation into the distribution and properties of histones and other basic proteins in bacteria

1966 ◽  
Vol 101 (3) ◽  
pp. 665-673 ◽  
Author(s):  
JL Leaver ◽  
HJ Cruft
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Gel Electrophoresis ◽  
Basic Protein ◽  
Starch Gel Electrophoresis ◽  
Basic Proteins ◽  
E Coli ◽  
Extraction And Purification ◽  
Starch Gel ◽  
Micro Organisms

1. Methods have been developed for the extraction and purification of bacterial basic proteins. These proteins were initially examined by a micro-method of starch-gel electrophoresis and were then characterized more fully. 2. Although it was found that most of the DNA in both Bacillus megaterium and Escherichia coli must be free from combination with basic protein, there was some evidence that a small portion might be in the form of a typical nucleohistone complex. 3. The ribosomes of both B. megaterium and E. coli were shown to contain approximately 2% of basic protein. On the basis of ultraviolet-absorption curves, partial amino acid analyses and their behaviour on electrophoresis in polyacrylamide gels, it was concluded that some of these ribosomal basic proteins may be extremely similar to typical histones. 4. These results are discussed in relation to those of other authors, and the possible functions of basic proteins present in micro-organisms are considered with reference to those that have already been proposed for the histones of higher organisms.

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