scholarly journals Phosphorylation and biosynthesis of high molecular weight proteins of tumor nuclear matrix

Cell Research ◽  
1998 ◽  
Vol 8 (3) ◽  
pp. 195-207 ◽  
Author(s):  
TM Bazarnova ◽  
TV Buldyaeva ◽  
LS Filatova ◽  
SB Akopov ◽  
IB Zbarsky
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Nuclear Matrix ◽  
High Molecular Weight Proteins

High Molecular Weight Proteins of Tumor Nuclear Matrix

1990 ◽  
pp. 355-359 ◽  
Author(s):  
I. B. Zbarsky ◽  
S. N. Kuzmina ◽  
T. V. Buldyaeva ◽  
T. M. Bazarnova
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Nuclear Matrix ◽  
High Molecular Weight Proteins

INTERFERENCE BY SERUM PROTEINS WITH LH RADIOIMMUNOASSAY USING IMMUNOSORBENT

1973 ◽  
Vol 72 (2) ◽  
pp. 235-242 ◽  
Author(s):  
A. M. Reuter ◽  
J. C. Hendrick ◽  
J. Sulon ◽  
P. Franchimont
Keyword(s):  
Molecular Weight ◽  
Human Serum ◽  
High Molecular Weight ◽  
Serum Proteins ◽  
Void Volume ◽  
High Molecular Weight Proteins ◽  
Serum Fractionation ◽  
Covalently Bound

ABSTRACT The percentage of LH* bound to antibodies that have been covalently bound to cellulose is diminished in the presence of LH-free human serum and sera from various species of animals. Serum fractionation studies on Sephadex G 200 show that the greatest interference comes from the proteins eluted in the void volume i. e. the high molecular weight proteins. Specifically, the gamma M globulins and the α2-macroglobulins appear to play an important role, as demonstrated by tests in which these proteins were neutralized by gamma M and α2-macroglobulin antisera.

scholarly journals Stereospecific Isotopic Labeling of Methyl Groups for NMR Spectroscopic Studies of High-Molecular-Weight Proteins

2010 ◽  
Vol 49 (11) ◽  
pp. 1958-1962 ◽  
Author(s):  
Pierre Gans ◽  
Olivier Hamelin ◽  
Remy Sounier ◽  
Isabel Ayala ◽  
M. Asunción Durá ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Isotopic Labeling ◽  
Spectroscopic Studies ◽  
Methyl Groups ◽  
High Molecular Weight Proteins

scholarly journals DNA and proteins of the nuclear matrix are the main targets of benzo[a]pyrene's action in rat hepatocytes.

1993 ◽  
Vol 40 (4) ◽  
pp. 559-562 ◽  
Author(s):  
P Widłak ◽  
J Rzeszowska-Wolny
Keyword(s):  
Molecular Weight ◽  
Dna Adducts ◽  
Dna Sequences ◽  
Nuclear Matrix ◽  
Rat Hepatocytes ◽  
The Other ◽  
Matrix Proteins ◽  
Nuclear Matrix Proteins ◽  
Cultured Rat Hepatocytes ◽  
High Molecular Weight Proteins

The binding of [14C]benzo[a]pyrene (B[a]P) to DNA and proteins in total nuclei and subnuclear fractions of cultured rat hepatocytes was compared. The main targets of B[a]P were non-histone high molecular weight proteins of the nuclear matrix and DNA sequences attached to this structure. Following 24 h exposure to B[a]P the amounts of adducts in the nuclear matrix DNA and proteins were twice as high as in total nuclei. After withdrawal of the carcinogen containing medium the level of B[a]P-induced adducts gradually decreased but always remained the highest in the nuclear matrix proteins. Removal of adducts from the nuclear matrix DNA was more efficient than from the other DNA fractions, and 72 h after exposure to the carcinogen the level of DNA adducts in this fraction was similar to that in total nuclei.

Influence of PEGylation on the Release of Low and High Molecular-Weight Proteins from PVA Matrices

1999 ◽  
Vol 14 (4) ◽  
pp. 315-330 ◽  
Author(s):  
F. M. Veronese ◽  
C. Mammucari ◽  
P. Caliceti ◽  
O. Schiavon ◽  
S. Lora
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
High Molecular Weight Proteins
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