scholarly journals Amino Acid Sequence of Cyanogen Bromide Fragment CN2 From a Hong Kong Influenza Haemagglutinin Heavy Chain

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.

1989 ◽  
Vol 54 (3) ◽  
pp. 803-810 ◽  
Author(s):  
Ivan Kluh ◽  
Ladislav Morávek ◽  
Manfred Pavlík

Cyanogen bromide fragment CB5 represents the region of the polypeptide chain of hemopexin between the fourth and fifth methionine residue (residues 232-352). It contains 120 amino acid residues in the following sequence: Arg-Cys-Ser-Pro-His-Leu-Val-Leu-Ser-Ala-Leu-Thr-Ser-Asp-Asn-His-Gly-Ala-Thr-Tyr-Ala-Phe-Ser-Gly-Thr-His-Tyr-Trp-Arg-Leu-Asp-Thr-Ser-Arg-Asp-Gly-Trp-His-Ser-Trp-Pro-Ile-Ala-His-Gln-Trp-Pro-Gln-Gly-Pro-Ser-Ala-Val-Asp-Ala-Ala-Phe-Ser-Trp-Glu-Glu-Lys-Leu-Tyr-Leu-Val-Gln-Gly-Thr-Gln-Val-Tyr-Val-Phe-Leu-Thr-Lys-Gly-Gly-Tyr-Thr-Leu-Val-Ser-Gly-Tyr-Pro-Lys-Arg-Leu-Glu-Lys-Glu-Val-Gly-Thr-Pro-His-Gly-Ile-Ile-Leu-Asp-Ser-Val-Asp-Ala-Ala-Phe-Ile-Cys-Pro-Gly-Ser-Ser-Arg-Leu-His-Ile-Met. The sequence was derived from the data on peptides prepared by cleavage of fragment CB5 by mild acid hydrolysis, by trypsin and chymotrypsin.


1980 ◽  
Vol 33 (3) ◽  
pp. 295 ◽  
Author(s):  
Keith H Gough ◽  
Adam S Inglis

The amino acid sequence of a 59-residue 'non-helical tail' from a low-sulfur microfibrillar protein (component 8c-I) from wool is reported. The amino acid composition shows relatively high contents of serine (17 %), half-cystine (14 %), proline (8 %), glycine (8 %) compared to the helical areas of component 8c-I. Although the composition of the cyanogen bromide fragment CNBr-3 resembles the compositions of the high-sulfur proteins extracted from wool there are no obvious sequence homologies present. The Edman degradation yields at an aspartyl-glycyl bond decreased so much that difficulties were encountered in determining the subsequent sequence.


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