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1981 (1)
1977 (1)
1Author    Ursula Yamaguchi-Koll, K. J. Wiegers, R. DrzeniekRequires cookie*
 Title    Dissociation and Reassociation of Poliovirus II. Protein Components Obtained by Urea Treatment of the Virus Particle  
 Abstract    Dissociation of poliovirus by 9 M urea in 0.015 M NaCl at 25 °C resulted in the liberation of 35S RNA and of polypeptides sedimenting at 2S in sucrose gradients containing 9 M urea. How­ ever. a ribonucleopolypeptide (RNPP) complex sedimenting at 45S and oligomers of the viral polypeptides sedimenting at 7 —8S were found in addition to the monomers sedimenting at 2S when the urea concentration was lowered to 5 M after the dissociation procedure. Ribonuclease treatment prevents the appearance of the RNPP-complex. The amount of the RNPP-complex de­ creased, when the dissociation was performed at higher ionic strength. Under these conditions small amounts of empty capsids were detected. Polyacrylamide gel electrophoresis showed that the RNPP-complex contained the polypeptide VP1. The oligomers (7 —8S) contained the polypeptide VP3 and small amounts of VP2. The bulk of VP2 and some VP3 were found in the 2S position together with VP4. The molecular weight of the dissociation products in urea and phosphate buffer was determined by gel filtration to be about 30,000 for the monomeric polypeptides containing predominantly VP2 and about 70,000 for the oligomeric polypeptides containing predominantly VP3. Our results demonstrate that the oligomers and the RNPP-complex are not primary products obtained by dissociation of the virus particle by urea but are due to a reassociation of the poly­ peptides or of VP1 and RNA. 
  Reference    (Z. Naturforsch. 32c, 632 [1977]; received December 12 1976/April 14 1977) 
  Published    1977 
  Keywords    Poliovirus, Dissociation Reassociation Protein Components, RNA-Protein Complex 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0632.pdf 
 Identifier    ZNC-1977-32c-0632 
 Volume    32 
2Author    Jochen Heukeshoven, Rudolf DemickRequires cookie*
 Title    Chemische Analyse und Struktur des Poliovirus. I. Cystein/Cystin Gehalt, vollständige Aminosäureanalyse und Hydrophobizität von Poliovirus und seinen natürlichen leeren Kapsiden Chemical Analysis and Structure of Poliovirus. I. Cysteine/Cystine Content, Complete Amino Acid Analysis and Hydrophobicity of Poliovirus and Its Naturally Occurring Empty Capsids  
 Abstract    The cysteine content o f poliovirus particles and naturally occuring empty capsids was determined by two methods: (1) reaction with vinylpyridine and subsequent amino acid analyses and (2) treatment with 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) and measurement in the change of absorption. Both methods were performed under dissociating conditions in order to expose all sulfhydryl groups. Poliovirus, type 1, strain Mahoney, contains 10-11 cysteine/cystine residues per protomer, irrespective o f the use o f virus particles or empty capsids. Poliovirus, type 3, strain Saukett, contains 1 2 -1 3 cysteine/cystine residues per protomer. Poliovirus particles are completely free o f disulfide bridges, whereas empty capsids contain 2 -4 cystine residues/protomer. N o sulfhydryl groups are present on the surface o f the virus particle, because of lack of reaction with DTNB. The tryptophan content was determined to be 13 ± 1 residues/protomer. By amino acid analysis under controlled hydrolyzing conditions 12 residues/protomer were found, whereas formylation in hydrochloric acid/formic acid revealed 14 residues/protomer; 13 tryptophan residues were calculated from the tyrosine-tryptophan relation and the optical density at 293.5 nm and 280 nm. The following parameters of poliovirus particles were calculated from the improved and complete amino acid analysis and the cysteine and tryptophan content: 1. The molecular weight of a protomer to be 92 700 ± 900 Dalton and of the poliovirus particle, type 1, strain Mahoney, to be 7.97 x 10® Dalton. 2. The relative hydrophobicity o f the poliovirus polypeptide to be 1.18. 3. The extinction coefficients o f poliovirus = 7 4 and o f empty capsids E\ g° = 16.2 ± 0.2. 
  Reference    Z. Naturforsch. 36c, 164—172 (1981); eingegangen am 21. August 1980 
  Published    1981 
  Keywords    Poliovirus, Empty Capsids, Amino Acid Analysis, Extinction Coefficient, Hydrophobicity 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0164.pdf 
 Identifier    ZNC-1981-36c-0164 
 Volume    36