Identification and purification of Namalwa nuclear RNP antigen 52/5.3

1983 ◽  
Vol 105 (1) ◽  
pp. 67-75 ◽  
Author(s):  
Kei Takahashi ◽  
Pui-Kwong Chan ◽  
Rose K. Busch ◽  
Harris Busch
Keyword(s):  
Rnp Antigen

Purification and Properties of the RNA Polymerase-Template Complex of an Influenza Virus

1973 ◽  
Vol 28 (3-4) ◽  
pp. 202-207 ◽  
Author(s):  
Ralph Τ. Schwarz ◽  
Christoph Scholtissek
Keyword(s):  
Rna Polymerase ◽  
Rna Synthesis ◽  
Lag Phase ◽  
Irreversible Loss ◽  
Enzyme Preparations ◽  
Purification And Properties ◽  
Virus Component ◽  
Template Complex ◽  
Rnp Antigen

The enzyme-template complex of influenza RNA polymerase (fowl plague virus) was purified 200-fold. The sole virus component found in this preparation was RNP-antigen. All attempts to remove the internal template led to an irreversible loss of enzyme activity. The complex was essentially free of nucleases. It synthesized exclusively viral minus strand RNA and was unable to initiate more than one cycle of RNA synthesis. The lag phase at the beginning of RNA synthesis in vitro, present in crude enzyme preparations, was abolished with the purified complex. The enzyme was sensitive to sulfhydryl reagents and it was able to accept α-S-ATP in place of ATP.

Antigenic studies on coronavirus. I. Identification of the structural antigens of human coronavirus, strain 229E

1981 ◽  
Vol 27 (3) ◽  
pp. 334-342 ◽  
Author(s):  
Shehab A. Yaseen ◽  
C. Margaret Johnson-Lussenburg
Keyword(s):  
Sodium Deoxycholate ◽  
Antigenic Analysis ◽  
Human Coronavirus ◽  
Specific Antigens ◽  
Integrated Or ◽  
Triton X ◽  
Rnp Antigen

Antigenic analysis of human coronavirus, strain 229E (HCV/229E), using a microimmunodiffusion technique, has resulted in the detection of six virion antigens. Comparison of the effect of several different virus-disrupting agents has shown that sodium deoxycholate or Triton X-100 were the best for HCV/229E disruption. Of the six coronavirion antigens, three were identified as virus specific and the remainder as host antigens, which were present as either integrated or nonspecifically adsorbed host components. One of the virus-specific antigens was identified as the internal nucleoprotein (229E/RNP). On the basis of immunodiffusion reactions with isolated 229E/RNP it was concluded that human convalescent sera reacted specifically with the 229E/RNP antigen.

scholarly journals Antibody penetration of viable human cells. II. Anti-RNP antibodies binding to RNP antigen expressed on cell surface, which may mediate the antibody internalization

1993 ◽  
Vol 93 (3) ◽  
pp. 396-404 ◽  
Author(s):  
J. MA ◽  
N. KING ◽  
S.-L. CHEN ◽  
R. PENNY ◽  
S. N. BREIT
Keyword(s):  
Cell Surface ◽  
Human Cells ◽  
Rnp Antigen

scholarly journals Binding of Ribonucleic Acids to the RNP-antigen Protein of Influenza Viruses

1971 ◽  
Vol 10 (1) ◽  
pp. 11-16 ◽  
Author(s):  
C. Scholtissek ◽  
H. Becht
Keyword(s):  
Influenza Viruses ◽  
Ribonucleic Acids ◽  
Antigen Protein ◽  
Rnp Antigen
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