The ubiquityl-calmodulin synthetase system from rabbit reticulocytes : isolation of the calmodulin-binding second component and enzymatic properties

1998 ◽  
Vol 255 (2) ◽  
pp. 492-500 ◽  
Author(s):  
Matthias Majetschak ◽  
Markus Laub ◽  
Christoph Klocke ◽  
Johannes A. Steppuhn ◽  
Herbert P. Jennissen
Keyword(s):  
Enzymatic Properties ◽  
Calmodulin Binding ◽  
Rabbit Reticulocytes

The structure of pre-mRNA and mRNA from erythroid cells

1978 ◽  
Vol 36 (2) ◽  
pp. 234-235
Author(s):  
A.-M. Ladhoff ◽  
B.J. Thiele ◽  
Ch. Coutelle ◽  
S. Rosenthal
Keyword(s):  
Bone Marrow ◽  
Structural Transformation ◽  
Electron Micrographs ◽  
Ammonium Acetate ◽  
Bone Marrow Cells ◽  
Erythroid Cells ◽  
Globin Mrna ◽  
Ordered Structures ◽  
Rabbit Bone ◽  
Rabbit Reticulocytes

The suggested precursor-product relationship between the nuclear pre-mRNA and the cytoplasmic mRNA has created increased interest also in the structure of these RNA species. Previously we have been published electron micrographs of individual pre-mRNA molecules from erythroid cells. An intersting observation was the appearance of a contour, probably corresponding to higher ordered structures, on one end of 10 % of the pre-mRNA molecules from erythroid rabbit bone marrow cells (Fig. 1A). A virtual similar contour was observed in molecules of 9S globin mRNA from rabbit reticulocytes (Fig. 1B). A structural transformation in a linear contour occurs if the RNA is heated for 10 min to 90°C in the presence of 80 % formamide. This structural transformation is reversible when the denatured RNA is precipitated and redissolved in 0.2 M ammonium acetate.

Three-dimensional reconstruction of the 40S ribosomal subunit from rabbit reticulocytes

1987 ◽  
Vol 45 ◽  
pp. 936-937
Author(s):  
Neng-Yu Zhang ◽  
Terence Wagenknecht ◽  
Michael Radermacher ◽  
Tom Obrig ◽  
Joachim Frank
Keyword(s):  
Three Dimensional ◽  
Ribosomal Subunit ◽  
Uranyl Acetate ◽  
Reconstruction Method ◽  
Single Exposure ◽  
Electron Dose ◽  
Ribosomal Subunits ◽  
40S Ribosomal Subunit ◽  
Dimensional Reconstruction ◽  
Rabbit Reticulocytes

We have reconstructed the 40S ribosomal subunit at a resolution of 4 nm using the single-exposure pseudo-conical reconstruction method of Radermacher et al.Small (40S) ribosomal subunits were Isolated from rabbit reticulocytes, applied to grids and negatively stained (0.5% uranyl acetate) in a manner that “sandwiches” the specimen between two layers of carbon. Regions of the grid exhibiting uniform and thick staining were identified and photographed twice (magnification 49,000X). The first micrograph was always taken with the specimen tilted by 50° and the second was of the Identical area untilted (Fig. 1). For each of the micrographs the specimen was subjected to an electron dose of 2000-3000 el/nm2.Three hundred thirty particles appearing in the L view (defined in [4]) were selected from both tilted- and untilted-specimen micrographs. The untilted particles were aligned and their rotational alignment produced the azimuthal angles of the tilted particles in the conical tilt series.

Enzymatic properties of mouse 25-hydroxyvitamin D3 1α-hydroxylase expressed in Escherichia coli

2001 ◽  
Vol 259 (3) ◽  
pp. 731-738 ◽  
Author(s):  
Toshiyuki Sakaki ◽  
Natsumi Sawada ◽  
Ken-ichi Takeyama ◽  
Shigeaki Kato ◽  
Kuniyo Inouye
Keyword(s):  
Escherichia Coli ◽  
Enzymatic Properties

Calmodulin binding agents from selected fungal metabolites

Planta Medica ◽  
2014 ◽  
Vol 80 (10) ◽  
Author(s):  
P Del Valle ◽  
M González-Andrade ◽  
M Figueroa ◽  
R Mata
Keyword(s):  
Fungal Metabolites ◽  
Calmodulin Binding ◽  
Binding Agents

scholarly journals Adult human liver contains intermediate-type proteasomes with different enzymatic properties

2014 ◽  
Vol 13 (4) ◽  
pp. 429-438 ◽  
Author(s):  
Sabrina Gohlke ◽  
Alexander Kloβ ◽  
Michael Tsokos ◽  
Kathrin Textoris-Taube ◽  
Christin Keller ◽  
...  
Keyword(s):  
Human Liver ◽  
Enzymatic Properties ◽  
Intermediate Type ◽  
Adult Human
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