Polynomial and Matrix Fraction Descriptions

2018 ◽  
pp. 153-174
Keyword(s):  
Matrix Fraction

The human L-myc gene encodes multiple nuclear phosphoproteins from alternatively processed mRNAs

1988 ◽  
Vol 8 (10) ◽  
pp. 4381-4388
Author(s):  
J De Greve ◽  
J Battey ◽  
J Fedorko ◽  
M Birrer ◽  
G Evan ◽  
...  
Keyword(s):  
Rna Processing ◽  
In Vitro Translation ◽  
Intron 1 ◽  
Myc Gene ◽  
Molecular Masses ◽  
Steady State Levels ◽  
Matrix Fraction ◽  
Nuclear Phosphoproteins

The human proto-oncogene L-myc generates at least four different mRNAs by alternative RNA processing. We have identified two phosphorylated L-myc proteins with molecular masses of 60,000 and 66,000 daltons [p60L-myc(human) and p66L-myc(human)] in a small-cell carcinoma line expressing high levels of L-myc mRNA. These proteins have a short half-life and are localized to the nuclear matrix fraction, as previously reported for the c-myc and N-myc proteins. In vitro translation experiments demonstrated that both the p60 and p66 species are encoded by a 3.9-kilobase (kb) mRNA which retains intron 1, while only the p60 protein is translated from a 3.6-kb L-myc mRNA which has had intron 1 removed. While L-myc proteins [p32L-myc(human) and p37L-myc(human)] could be synthesized in vitro from 2.2-kb mRNA templates, no such proteins were detected by immunoprecipitation in vivo. These observations suggest that alternative RNA processing of the L-myc transcript could play a role in determining the steady-state levels of the p60L-myc and p66L-myc proteins.

scholarly journals Matrix-fraction description from frequency samples

1993 ◽  
Vol 181 ◽  
pp. 251-268 ◽  
Author(s):  
D.W. Richardson ◽  
B.D.O. Anderson ◽  
N.K. Bose
Keyword(s):  
Matrix Fraction

scholarly journals BIOCHEMICAL AND ULTRASTRUCTURAL PROPERTIES OF A MITOCHONDRIAL INNER MEMBRANE FRACTION DEFICIENT IN OUTER MEMBRANE AND MATRIX ACTIVITIES

1970 ◽  
Vol 45 (2) ◽  
pp. 291-305 ◽  
Author(s):  
T. L. Chan ◽  
John W. Greenawalt ◽  
Peter L. Pedersen
Keyword(s):  
Outer Membrane ◽  
Membrane Fraction ◽  
Phosphorylation Site ◽  
Membrane Vesicles ◽  
Rat Liver Mitochondria ◽  
Mitochondrial Activity ◽  
Inner Membrane ◽  
Membrane Matrix ◽  
Matrix Fraction ◽  
Stimulation Of

Treatment of the inner membrane matrix fraction of rat liver mitochondria with the nonionic detergent Lubrol WX solubilized about 70% of the total protein and 90% or more of the following matrix activities: malate dehydrogenase, glutamate dehydrogenase, and isocitrate dehydrogenase (NADP). The Lubrol-insoluble fraction was enriched in cytochromes, phospholipids, and a Mg++-stimulated ATPase activity. Less than 2% of the total mitochondrial activity of monoamine oxidase, an outer membrane marker, or adenylate kinase, an intracristal space marker could be detected in this inner membrane fraction. Electron micrographs of negatively stained preparations showed vesicles (≤0.4 µ diameter) literally saturated on the periphery with the 90 A ATPase particles. These inner membrane vesicles, which appeared for the most part to be inverted with respect to the normal inner membrane configuration in intact mitochondria, retained the succinicoxidase portion of the electron-transport chain, an intact phosphorylation site II with a high affinity for ADP, and the capacity to accumulate Ca++. A number of biochemical properties characteristic of intact mitochondria and the inner membrane matrix fraction, however, were either absent or markedly deficient in the inner membrane vesicles. These included stimulation of respiration by either ADP or 2,4-dinitrophenol, oligomycin-sensitive ADP-ATP exchange activity, atractyloside sensitivity of adenine nucleotide requiring reactions, and a stimulation of the Mg++-ATPase by 2,4-dinitrophenol.

System zeros determination from an unreduced matrix fraction description

1993 ◽  
Vol 38 (11) ◽  
pp. 1695-1697
Author(s):  
K.S. Yeung ◽  
Chi-Man Kwan
Keyword(s):  
Matrix Fraction
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