A Simple Fractionation Procedure for Histones by Block Cellogel Electrophoresis

1975 ◽  
Vol 3 (6) ◽  
pp. 1012-1012
Author(s):  
FAUSTO MACHICAO ◽  
JOHANN SONNENBICHLER
Keyword(s):  
Fractionation Procedure ◽  
Cellogel Electrophoresis

An Evaluation of a Plasma Fractionation System

1960 ◽  
Vol 4 (01) ◽  
pp. 031-044
Author(s):  
George Y. Shinowara ◽  
E. Mary Ruth
Keyword(s):  
Biological Activity ◽  
Ionic Strength ◽  
Plasma Proteins ◽  
High Concentration ◽  
Significant Evidence ◽  
Native Proteins ◽  
Mobility Data ◽  
Fractionation Procedure ◽  
The Individual ◽  
Low Ionic Strength

SummaryFour primary fractions comprising at least 97 per cent of the plasma proteins have been critically appraised for evidence of denaturation arising from a low temperature—low ionic strength fractionation system. The results in addition to those referable to the recovery of mass and biological activity include the following: The high solubilities of these fractions at pH 7.3 and low ionic strengths; the compatibility of the electrophoretic and ultracentrifugal data of the individual fractions with those of the original plasma; and the recovery of hemoglobin, not hematin, in fraction III obtained from specimens contaminated with this pigment. However, the most significant evidence for minimum alterations of native proteins was that the S20, w and the electrophoretic mobility data on the physically recombined fractions were identical to those found on whole plasma.The fractionation procedure examined here quantitatively isolates fibrinogen, prothrombin and antithrombin in primary fractions. Results have been obtained demonstrating its significance in other biological systems. These include the following: The finding of 5 S20, w classes in the 4 primary fractions; the occurrence of more than 90 per cent of the plasma gamma globulins in fraction III; the 98 per cent pure albumin in fraction IV; and, finally, the high concentration of beta lipoproteins in fraction II.

CHANGES WITH TIME IN THE FORM AND AVAILABILITY OF RESIDUAL FERTILIZER PHOSPHORUS ON CHERNOZEMIC SOILS

1986 ◽  
Vol 66 (1) ◽  
pp. 105-119 ◽  
Author(s):  
B. I. WAGAR ◽  
J. W. B. STEWART ◽  
J. O. MOIR
Keyword(s):  
Key Words ◽  
Organic P ◽  
Clay Loam ◽  
P Fractionation ◽  
Residual P ◽  
Fractionation Procedure ◽  
P Fertilizer ◽  
Labile P ◽  
P Transformations ◽  
Stable Forms

A sequential phosphorus (P) fractionation procedure was used to measure the changes in the labile and stable forms of inorganic and organic P following single broadcast P applications to Canadian Chernozemic soils under cereal cropping. Approximately half of the fertilizer residues remained in plant-available forms (resin, NaHCO3). In a Black Waskada clay loam 8 yr after the application of 200 and 400 kg P ha−1, residual fertilizer P consisted of resin-P, 30–40%; HCl-P, 25–30%; residue-P, 10–15%; NaOH-P, 10–15%, NaHCO3-P, 10%; and aggregate protected P, 3%. The residues in a Dark Brown Sutherland clay 5 yr after the application of 160 kg P ha−1 were: resin-P, 35%; NaOH-P, 30–40%; NaHCO3-P, 15%; HCl-P, 0–5%; H2SO4-P, 5%; and aggregate protected P, 5%. The soils differed in the quantity of fertilizer recovered in inorganic HCl-extractable forms. In the Sutherland soil the change from wheat-fallow to continuous wheat cropping produced a build-up of organic P which occurred with and without the addition of P fertilizer. Key words: Residual P, P transformations, Labile Pi; labile Po, stable Pi stable Po

Relationship between phosphorus fractions and properties of highly calcareous soils

Soil Research ◽  
2007 ◽  
Vol 45 (4) ◽  
pp. 255 ◽  
Author(s):  
Ebrahim Adhami ◽  
Hamid Reza Memarian ◽  
Farzad Rassaei ◽  
Ehsan Mahdavi ◽  
Manouchehr Maftoun ◽  
...  
Keyword(s):  
Calcareous Soils ◽  
Hydroxylamine Hydrochloride ◽  
Inorganic Phosphorus ◽  
Influential Factor ◽  
Sequential Fractionation ◽  
Inorganic P ◽  
Soil P ◽  
Fractionation Procedure ◽  
Extractable P ◽  
P Content

Inorganic phosphorus (P) sequential fractionation schemes are applicable techniques to interpret soil P status. The present study was initiated to determine the origin of various P fractions in highly calcareous soils. Inorganic P forms were determined by a sequential fractionation procedure extracting with NaOH (NaOH-P), Na citrate-bicarbonate (CB-P), Na citrate 2 times (C1-P and C2-P), Na citrate-ascorbate (CAs-P), Na citrate-bicarbonate-dithionite (CBD-P), Na acetate (NaAc-P), and HCl (HCl-P). Results showed that NaOH-P was negatively correlated with active iron oxides. CB-P was positively correlated with silt content and negatively related to citrate-bicarbonate-dithionite extractable Fe (Fed). This result illustrates the weathering effect on Ca-P, with Ca-P content declining as a consequence of weathering. A negative correlation was observed between C1-P and citrate ascorbate extractable Fe (FeCAs). Second citrate extractable P (C2-P) was negatively related to calcium carbonate equivalent and positively related to hydroxylamine-hydrochloride and neutral ammonium acetate-hydroquinone extractable Mn (Mnh and Mnq). Fine silt (Fsilt) was the most influential factor affecting CAs-P. It seemed citrate-dithionite-bicarbonate extractable Al (Ald), Mnh, and Mnq have been sinks for CBD-P, while free iron oxide compounds (Feo, Fec, and FeCAs) were a major contributing factor for the formation of NaAc-P. Stable P compounds (HCl-P) of highly calcareous soils originated from coarse silt (Csilt) and hydroxylamine-hydrochloride extractable Mn (Mnh).

scholarly journals Halobacterium cutirubrum ribosomes. Properties of the ribosomal proteins and ribonucleic acid

1972 ◽  
Vol 130 (1) ◽  
pp. 103-110 ◽  
Author(s):  
L. P. Visentin ◽  
C. Chow ◽  
A. T. Matheson ◽  
M. Yaguchi ◽  
F. Rollin
Keyword(s):  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Soluble Fraction ◽  
Ribosomal Subunit ◽  
23S Rrna ◽  
Core Particle ◽  
Fractionation Procedure ◽  
Additional Protein ◽  
70S Ribosome ◽  
Low Ionic Strength

1. The 30S ribosomal subunit of the extreme halophile Halobacterium cutirubrum is unstable and loses 75% of its ribosomal protein when the 70S ribosome is dissociated into the two subunits. A stable 30S subunit is obtained if the dissociation of the 70S particle is carried out in the presence of the soluble fraction. 2. A fractionation procedure was developed for the selective removal of groups of proteins from the 30S and 50S subunits. When the ribosomes, which are stable in 4m-K+ and 0.1m-Mg2+, were extracted with low-ionic-strength buffer 75–80% of the 30S proteins and 60–65% of the 50S proteins as well as the 5S rRNA were released. The proteins in this fraction are the most acidic of the H. cutirubrum ribosomal proteins. Further extraction with Li+–EDTA releases additional protein, leaving a core particle containing either 16S rRNA or 23S rRNA and about 5% of the total ribosomal protein. The amino acid composition, mobility on polyacrylamide gels at pH4.5 and 8.7, and the molecular-weight distribution of the various protein fractions were determined. 3. The s values of the rRNA are 5S, 16S and 23S. The C+G contents of the 16S and 23S rRNA were 56.1 and 58.8% respectively and these are higher than C+G contents of the corresponding Escherichia coli rRNA (53.8 and 54.1%).

A modified fractionation procedure for avian erythrocyte histones

1969 ◽  
Vol 47 (12) ◽  
pp. 1121-1123 ◽  
Author(s):  
G. H. M. Adams ◽  
J. M. Neelin
Keyword(s):  
Cation Exchange ◽  
Exchange Chromatography ◽  
Cation Exchange Chromatography ◽  
Fractionation Procedure ◽  
Exclusion Chromatography ◽  
One Step ◽  
Avian Erythrocyte ◽  
Fractionation Method ◽  
Time Required

The fractionation method of Vidali and Neelin for avian erythrocyte histones was modified to reduce the time required to obtain clean fractions of serine-rich and arginine-rich histones. Histones were extracted from washed nuclei in one step with 0.20 M HCl. The lysine-rich and the moderately lysine-rich histones were fractionated by cation-exchange chromatography but the serine-rich and arginine-rich histones were eluted together. These histones were separated by subsequent exclusion chromatography.

Characterization of a novel 63 kDa membrane protein. Implications for the organization of the ER-to-Golgi pathway

1993 ◽  
Vol 104 (3) ◽  
pp. 671-683 ◽  
Author(s):  
A. Schweizer ◽  
M. Ericsson ◽  
T. Bachi ◽  
G. Griffiths ◽  
H.P. Hauri
Keyword(s):  
Membrane Protein ◽  
Laser Scanning ◽  
Protein Transport ◽  
Brefeldin A ◽  
Vero Cells ◽  
Subcellular Fractionation ◽  
Confocal Laser ◽  
Similar Degree ◽  
Fractionation Procedure ◽  
Intermediate Compartment

Owing to the lack of appropriate markers the structural organization of the ER-to-Golgi pathway and the dynamics of its membrane elements have been elusive. To elucidate this organization we have taken a monoclonal antibody (mAb) approach. A mAb against a novel 63 kDa membrane protein (p63) was produced that identifies a large tubular network of smooth membranes in the cytoplasm of primate cells. The distribution of p63 overlaps with the ER-Golgi intermediate compartment, defined by a previously described 53 kDa marker protein (here termed ERGIC-53), as visualized by confocal laser scanning immunofluorescence microscopy and immunoelectron microscopy. The p63 compartment mediates protein transport from the ER to Golgi apparatus, as indicated by partial colocalization of p63 and vesicular stomatitis virus G protein in Vero cells cultured at 15 degrees C. Low temperatures and brefeldin A had little effect on the cellular distribution of p63, suggesting that this novel marker is a stably anchored resident protein of these pre-Golgi membranes. p63 and ERGIC-53 were enriched to a similar degree by the same subcellular fractionation procedure. These findings demonstrate an unanticipated complexity of the ER-Golgi interface and suggest that the ER-Golgi intermediate compartment defined by ERGIC-53 may be part of a greater network of smooth membranes.

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