An Antigenic Site of Sperm Whale Myoglobin

Nature ◽  
1967 ◽  
Vol 215 (5096) ◽  
pp. 17-20 ◽  
Author(s):  
M. J. CRUMPTON
Keyword(s):  
Antigenic Site ◽  
Sperm Whale ◽  
Sperm Whale Myoglobin

scholarly journals Nearest-neighbour analysis of myoglobin antigenic sites. Nearest-neighbour residues whose replacement can alter the environment of binding-site residue(s) and thus change their characteristics and binding capability

1980 ◽  
Vol 191 (3) ◽  
pp. 673-680 ◽  
Author(s):  
A L Kazim ◽  
M Z Atassi
Keyword(s):  
Binding Capacity ◽  
Antigenic Site ◽  
Sperm Whale ◽  
Antigenic Structure ◽  
Nearest Neighbour ◽  
X Ray ◽  
Antigenic Sites ◽  
Binding Capability ◽  
Sperm Whale Myoglobin ◽  
Neighbour Analysis

By using the known antigenic structure of sperm-whale myoglobin previously determined in this laboratory and the X-ray co-ordinates for the myoglobin molecule, we have calculated the nearest-atom distances between each of the residues of the antigenic sites and all the other amino acids of the myoglobin molecule. These calculations have enabled us to identify the nearest-neighbour residues to each of the residues in the five antigenic sites, and which thus describe the immediate molecular environment of the sites. The influences of chemical changes or replacements in these environmental residues on the binding capacity of an antigenic site, when considered together with replacements directly in the antigenic sites, are expected to account for the major effects and will be extremely useful in explaining the cross-reactions of myoglobins from various species. However, it is stressed that the analysis has limitations due to the qualitative estimates of the effects, the influences of substitutions of once-removed or even at more distant locations (especially when they are cumulative) and finally the influences of any conformational re-adjustments when these occur as a result of the replacement(s).

scholarly journals The immunological activity of some of the chymotryptic peptides of sperm-whale myoglobin

1965 ◽  
Vol 94 (3) ◽  
pp. 545-556 ◽  
Author(s):  
MJ Crumpton ◽  
JM Wilkinson
Keyword(s):  
Amino Acid ◽  
Antigenic Site ◽  
Molecular Size ◽  
Sperm Whale ◽  
Exchange Chromatography ◽  
Amino Acid Sequences ◽  
Molecular Weights ◽  
Molar Ratios ◽  
A Minor ◽  
Sperm Whale Myoglobin

1. Sperm-whale apomyoglobin was digested with chymotrypsin in a dialysis sac. The ultrafiltrate contained incompletely hydrolysed fragments which partially inhibited the precipitation of metmyoglobin and apomyoglobin by some antisera produced against metmyoglobin. The inhibitory activity was stable to heating at 100 degrees and depended on the peptide structure. 2. The fragments were fractionated according to molecular size and were purified by ion-exchange chromatography. Six pure peptides and two peptides which contained a minor impurity were isolated. Their amino acid compositions and N-terminal amino acid sequences were determined and their entire amino acid sequences deduced from the known amino acid sequence of sperm-whale myoglobin. 3. The peptides formed no detectable precipitates with the antisera. Five of the eight peptides partially inhibited the precipitation of apomyoglobin and/or metmyoglobin by one antiserum. Six of the peptides inhibited the precipitation of apomyoglobin by one or other of two antisera; at least two of these peptides inhibited both antisera. One peptide failed to inhibit the precipitation of either antigen by either antiserum. Two of the peptides possessed the same serological specificity. 4. The molar ratios of inhibitors to antigen for 50% of the maximum inhibition decreased as the molecular size of the inhibitor increased. With one antiserum and with apomyoglobin as the antigen, molar ratios 12 and 80 were obtained for peptides with molecular weights 2051 and 793 respectively. 5. The size and structure of an antigenic site is discussed in relation to the known steric configuration of myoglobin.

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