LOCALIZATION OF 2',3'-CYCLIC NUCLEOTIDE-3'-PHOSPHOHYDROLASE OF RABBIT BRAIN BY SEDIMENTATION IN A CONTINUOUS SUCROSE GRADIENT

1978 ◽  
Vol 30 (4) ◽  
pp. 735-744 ◽  
Author(s):  
R. Shapira ◽  
W. C. Mobley ◽  
S. B. Thiele ◽  
M. R. Wilhelmi ◽  
A. Wallace ◽  
...  
Keyword(s):  
Cyclic Nucleotide ◽  
Sucrose Gradient ◽  
Rabbit Brain ◽  
Continuous Sucrose Gradient

Preparation of Purified Myelin of Rabbit Brain by Sedimentation in a Continuous Sucrose Gradient

1970 ◽  
Vol 133 (1) ◽  
pp. 238-245 ◽  
Author(s):  
R. Shapira ◽  
F. Binkley ◽  
R. F. Kibler ◽  
I. J. Wundram
Keyword(s):  
Sucrose Gradient ◽  
Rabbit Brain ◽  
Continuous Sucrose Gradient

scholarly journals Two enzymes involved in the synthesis of O-linked oligosaccharides are localized on membranes of different densities in mouse lymphoma BW5147 cells.

1984 ◽  
Vol 99 (1) ◽  
pp. 327-331 ◽  
Author(s):  
A Elhammer ◽  
S Kornfeld
Keyword(s):  
Endoplasmic Reticulum ◽  
Membrane Fraction ◽  
Sucrose Gradient ◽  
Marker Enzymes ◽  
Continuous Sucrose Gradient ◽  
Microsomal Membranes ◽  
Intermediate Density ◽  
Mouse Lymphoma

Microsomal membranes from mouse lymphoma BW5147 cells were fractionated on a continuous sucrose gradient and assayed for two enzymes involved in the synthesis of O-linked oligosaccharides. Both enzymes were recovered in membranes that were less dense than the membranes containing the endoplasmic reticulum marker enzymes, glucosidase I and II. UDP-Gal:N-acetylgalactosamine-beta 1, 3-galactosyltransferase had a distribution that coincided with that of the galactosyltransferase that acts on asparagine-linked oligosaccharides. This latter enzyme has been immunolocalized to the trans Golgi elements. The UDP-GalNAc:polypeptide N-acetylgalactosaminyl-transferase was recovered in a membrane fraction of intermediate density, between the endoplasmic reticulum and trans Golgi markers. These findings are consistent with the assembly of O-linked oligosaccharides occurring in at least two different Golgi compartments.

scholarly journals Association of the Two Glycosyl Transferase Activities of Glycoprotein Synthesis with Low Equilibrium Density Smooth Microsomes

1973 ◽  
Vol 12 (2) ◽  
pp. 603-615
Author(s):  
R. R. WAGNER ◽  
ELISABETH PETTERSSON ◽  
G. DALLNER
Keyword(s):  
Sucrose Gradient ◽  
Microsomal Fraction ◽  
Equilibrium Density ◽  
Separate Entity ◽  
Broad Distribution ◽  
Glycoprotein Synthesis ◽  
Cellular Origin ◽  
Galactosyl Transferase ◽  
Oligosaccharide Chain ◽  
Continuous Sucrose Gradient

Smooth microsomes of rat liver were subfractionated on a continuous sucrose gradient to isopycnic equilibrium density. All the microsomal electron-transport enzymes and phosphatases exhibit a broad distribution in the various microsomal subfractions. On the other hand, the N-acetylglucosaminyl and galactosyl transferase activities, which are known to participate in the synthesis of the oligosaccharide chain of the plasma glycoproteins, exhibit a markedly different distribution pattern. They are concentrated to a small fraction having an isopycnic equilibrium density of 1.10. These membranes represent a separate entity of the smooth microsomal fraction, the exact cellular origin of which remains to be clarified.

scholarly journals The construction and analysis of sucrose gradients for use with zonal rotors

1976 ◽  
Vol 159 (2) ◽  
pp. 259-265 ◽  
Author(s):  
W Hirst ◽  
R A Cox
Keyword(s):  
Iterative Procedure ◽  
Sucrose Gradient ◽  
Sucrose Solution ◽  
Sucrose Concentration ◽  
Gradient Centrifugation ◽  
Sedimentation Coefficient ◽  
Sucrose Gradient Centrifugation ◽  
Comparison With Experiment ◽  
Continuous Sucrose Gradient ◽  
Simple Equations

The rate of sedimentation of a particle in a sucrose solution depends on the viscosity and density of the medium. These two variables are related to the sucrose concentration and the temperature of the medium by new simple equations. These equations were used in a rapid iterative procedure that relates the distance moved by a zone in a continuous sucrose gradient to its sedimentation coefficient. It is shown by comparison with experiment that this iterative method allows the distance moved by a zone to be calculated rapidly. The method may therefore be used to optimize the separation of particles in a sucrose-gradient-centrifugation experiment. The method also allows the unknown sedimentation coefficients of several zones to be measured from a single sucrose-gradient-centrifugation experiment.

scholarly journals High content of tyrosine and arginine in peptides and proteins from the growth hormone producing cells of the adenohypophysis.

1980 ◽  
Vol 28 (5) ◽  
pp. 401-407 ◽  
Author(s):  
R Ekman ◽  
R Håkanson ◽  
F Sundler ◽  
J Thorell
Keyword(s):  
Growth Hormone ◽  
Sucrose Gradient ◽  
Gel Chromatography ◽  
Molecular Weights ◽  
Continuous Sucrose Gradient ◽  
Arginine Residues ◽  
Rich Material ◽  
Soluble Components ◽  
Millipore Filters ◽  
Pig Pituitaries

Fluorescence histochemistry has demonstrated an abundance of tyrosine and arginine residues in the growth hormone (GH) producing cells of the pituitary of several mammals. Granules from pig pituitaries were purified by passage through a succession of Millipore filters followed by centrifugation on a continuous sucrose gradient. One granular fraction, rich in GH, was found to contain proteins or peptides rich in tyrosine and arginine. Gel chromatography of the acid-soluble components from sedimented pituitary granules revealed that the arginine- and tyrosine-rich material was heterogeneous. The arginine-containing peptides and proteins could be separated into several peaks with molecular weights from 5000-10,000 and higher. The tyrosine-containing material comprised one peptide with a molecular weight of 5000-10,000 and another much smaller peptide. Since GH itself is not excessively rich in either tyrosine or arginine, the tyrosine- and arginine-containing proteins or peptides probably constitute as yet unidentified granular components, distinct from GH itself.

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