Covalent structure of a human γG-immunoglobulin. VII. Amino acid sequence of heavy-chain cyanogen bromide fragments H1-H4

Biochemistry ◽  
1970 ◽  
Vol 9 (16) ◽  
pp. 3161-3170 ◽  
Author(s):  
Bruce A. Cunningham ◽  
Urs S. Rutishauser ◽  
W. Einar Gall ◽  
Paul D. Gottlieb ◽  
Myron J. Waxdal ◽  
...  
Biochemistry ◽  
1970 ◽  
Vol 9 (16) ◽  
pp. 3171-3181 ◽  
Author(s):  
Urs S. Rutishauser ◽  
Bruce A. Cunningham ◽  
Carl Bennett ◽  
William Konigsberg ◽  
Gerald M. Edelman

1980 ◽  
Vol 33 (2) ◽  
pp. 137 ◽  
Author(s):  
Colin W Ward ◽  
Theo AA Dopheide ◽  
Adam S Inglis

The amino acid sequence of cyanogen bromide peptide CN2 from the heavy chain (HAl) of the haemagglutinin of the Hong Kong variant A/Memphis/l02/72 has been obtained by direct, automated sequence analysis on the whole fragment and by manual dansyl-Edman degradation of tryptic, peptic and chymotryptic peptides. It was found to contain 92 amino acid residues, including a large, insoluble, tryptic core peptide (residues 62-87). It did not contain any half-cystine residues or carbohydrate. The determination of its structure was complicated by the presence of an Asn-Ile bond at positions 48-49 which was readily cleaved by both trypsin and chymotrypsin.


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