The high-molecular-weight proteins of bovine brain plain synaptic vesicles

1987 ◽  
Vol 12 (7) ◽  
pp. 635-640
Author(s):  
Paul E. March ◽  
Edna Antonian ◽  
Diane M. Schneider ◽  
David M. Rothwarf ◽  
Edward R. Thornton
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Synaptic Vesicles ◽  
Bovine Brain ◽  
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

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

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

High molecular weight polypeptides related to dynein heavy chains in Nicotiana tabacum pollen tubes

1995 ◽  
Vol 108 (3) ◽  
pp. 1117-1125
Author(s):  
A. Moscatelli ◽  
C. Del Casino ◽  
L. Lozzi ◽  
G. Cai ◽  
M. Scali ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Nicotiana Tabacum ◽  
Pollen Tube ◽  
High Molecular Weight ◽  
Pollen Tubes ◽  
Biochemical Properties ◽  
Bovine Brain ◽  
Atp Binding ◽  
Heavy Chains ◽  
Dynein Heavy Chains

Nicotiana tabacum pollen tubes contain two high molecular weight polypeptides (about 400 kDa), which are specifically expressed during pollen germination and pollen tube growth in BK medium. The high molecular weight doublet resembles the dynein heavy chains in some biochemical properties. Sedimentation profiles of pollen tube extracts show that the high molecular weight bands have sedimentation coefficients of 22 S and 12 S, respectively. ATPase assay of sedimentation fractions shows an activity ten times higher when stimulated by the presence of bovine brain microtubules in fractions containing the 22 S high molecular weight polypeptide. Both these high molecular weight polypeptides can bind microtubules in an ATP-dependent fashion. A mouse antiserum to a synthetic peptide reproducing the sequence of the most conserved ATP-binding site among dynein heavy chains recognized the two high molecular weight polypeptides. Therefore these polypeptides have sequences immunologically related to the ATP binding sites of dynein heavy chains.

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