Characterization of hog cholera virus II. Determination of sedimentation coefficient

1967 ◽  
Vol 21 (3-4) ◽  
pp. 447-453 ◽  
Author(s):  
M. Horzinek
Keyword(s):  
Sedimentation Coefficient ◽  
Hog Cholera ◽  
Hog Cholera Virus

Characterization of the hog cholera virus 5′ terminus

Virus Genes ◽  
1995 ◽  
Vol 10 (2) ◽  
pp. 185-187 ◽  
Author(s):  
Kazuhiko Katayama ◽  
Chie Kurihara ◽  
Shuetsu Fukushi ◽  
Fuminori B. Hoshino ◽  
Kiyoyasu Ishikawa ◽  
...  
Keyword(s):  
Hog Cholera ◽  
Hog Cholera Virus

Expression and Characterization of Part of Hog Cholera Virus Non-structural Proteins

1996 ◽  
Vol 43 (1-10) ◽  
pp. 167-177
Author(s):  
L. Bakkali Kassimi ◽  
M. Gonzague ◽  
A. Boutrouille ◽  
C. Cruciere
Keyword(s):  
Structural Proteins ◽  
Hog Cholera ◽  
Hog Cholera Virus

Production and characterization of monoclonal antibodies against hog cholera virus (Alfort 187 strain)

1993 ◽  
Vol 131 (1-2) ◽  
pp. 185-192 ◽  
Author(s):  
A. Caij ◽  
G. Muyldermans ◽  
A. De Smet ◽  
R. Hamers ◽  
F. Koenen
Keyword(s):  
Monoclonal Antibodies ◽  
Hog Cholera ◽  
Hog Cholera Virus

scholarly journals Haemoglobin from the tadpole shrimp, Lepidurus apus lubbocki Characterization of the molecule and determination of the number of polypeptide chains

1979 ◽  
Vol 183 (2) ◽  
pp. 325-330 ◽  
Author(s):  
E Ilan ◽  
E Daniel
Keyword(s):  
Molecular Weight ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Sedimentation Coefficient ◽  
Sedimentation Equilibrium ◽  
Guanidinium Chloride ◽  
Tadpole Shrimp ◽  
Polypeptide Chains

Haemoglobin from the tadpole shrimp, Lepidurus apus lubbocki, was found to have a sedimentation coefficient (s020,w) of 19.3 +/- 0.2 S and a molecular weight, as determined by sedimentation equilibrium, of 798000 +/- 20000. The amino acid composition showed the lack of cysteine and cystine residues. A haem content of 3.55 +/- 0.03% was determined, corresponding to a minimal mol.wt. of 17400 +/- 200. The pH-independence in the range pH 5-11 of the sedimentation coefficient indicates a relatively high stability of the native molecule. Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis gave one band with mobility corresponding to a mol.wt. of 34000 +/- 1500. The molecular weight of the polypeptide chain was determined to be 32800 +/- 800 by sedimentation equilibrium in 6 M-guanidinium chloride and 0.1 M-2-mercaptoethanol. The findings indicate that Lepidurus haemoglobin is composed of 24 identical polypeptide chains, carrying two haem groups each.

Characterization of structural and non-structural proteins of hog cholera virus by means of monoclonal antibodies

1993 ◽  
Vol 131 (3-4) ◽  
pp. 405-417 ◽  
Author(s):  
G. Muyldermans ◽  
A. Caij ◽  
A. De Smet ◽  
F. Koenen ◽  
R. Hamers
Keyword(s):  
Monoclonal Antibodies ◽  
Structural Proteins ◽  
Hog Cholera ◽  
Hog Cholera Virus

Hog cholera virus—characterization of specific antiserum and identification of cDNA clones

Virology ◽  
1989 ◽  
Vol 171 (1) ◽  
pp. 18-27 ◽  
Author(s):  
Tillmann Rümenapf ◽  
Gregor Meyers ◽  
Robert Stark ◽  
Heinz-Jürgen Thiel
Keyword(s):  
Specific Antiserum ◽  
Cdna Clones ◽  
Hog Cholera ◽  
Hog Cholera Virus

Investigation of drug-protein interactions and the drug-carrier concept by the use of branched polypeptides as model systems. Synthesis and characterization of the model peptides

1980 ◽  
Vol 45 (3) ◽  
pp. 933-940 ◽  
Author(s):  
Ferenc Hudecz ◽  
Mária Szekerke
Keyword(s):  
Amino Acids ◽  
Protein Interactions ◽  
Drug Carrier ◽  
Sedimentation Coefficient ◽  
Model Systems ◽  
Gel Chromatography ◽  
Weight Estimation ◽  
Active Ester

Synthesis of branched polypeptides with a new design of variations in surface topography is described. The side chains of the poly(Lys-(DL-Alam)) were elongated by single amino acids (L-Tyr, L-Glu, L-His, L-Leu, L-Pro, L-Phe) or short polymers (L-, D-Glu, L-Tyr, L-, D-, DL-Lys). Single amino acids were coupled, via the azide, active ester or N-carboxy anhydride method, oligomers were grafted by the polymerisation of N-carboxy anhydride derivatives. The resulting polypeptides were characterised by amino acid analysis, identification of the N-terminal residue of the chain ends, determination of the sedimentation coefficient and molecular weight estimation, based on sedimentation experiments and thin layer gel chromatography.

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