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1981 (1)
1980 (1)
1Author    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 
2Author    Abteilung Biochemie, C.H Boehringer SohnRequires cookie*
 Title    B. Schöbel und W. Pollmann  
 Abstract    In addition to our previous paper [1] further characteristics of the chlorogenic acid hydrolase are described. Polyacrylamid gelelectrophoresis revealed only one band for the purified enzyme. Sodium dodecyl-sulfate polyacrylamid gelelectrophoresis showed a molecular weight of 60000, demonstrating four subunits o f the enzyme (total molecular weight 240000). The enzyme is stable in a pH-range of 3 .0 -8 .5 and up to a temperature o f 55 °C. The temperature coefficient Q10 is 1.5, the activation energy EA is 6.0 kcal/mol. The amino acid analysis and substrate specificity data are given in tables. Essential for the enzyme activity is the C=C double bound neighbouring the ester linkage. The enzyme crystallizes in prisms. Weitere Charakterisierung einer Chlorogensäure-Hydrolase aus Aspergillus niger 
  Reference    Z. Naturforsch. 35c, 699—701 (1980); eingegangen am 12. Mai/20. Juni 1980 
  Published    1980 
  Keywords    Chlorogenic Acid Hydrolase, Aspergillus niger, Polyacrylamid Gelelectrophoresis, Amino Acid Analysis, Substrate Specificity 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0699.pdf 
 Identifier    ZNC-1980-35c-0699 
 Volume    35