scholarly journals Complete Amino Acid Sequence of the N-Terminal Cyanogen Bromide Fragment CNBr-3 From a Microfibrillar Protein From Wool

1980 ◽  
Vol 33 (3) ◽  
pp. 295 ◽  
Author(s):  
Keith H Gough ◽  
Adam S Inglis
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Cyanogen Bromide ◽  
Edman Degradation ◽  
Complete Amino Acid Sequence ◽  
Sequence Homologies ◽  
Low Sulfur ◽  
Cyanogen Bromide Fragment

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.

Amino acid sequence differences in the alpha chains of pea seed isolectins: C-terminal processing

1987 ◽  
Vol 65 (4) ◽  
pp. 338-344 ◽  
Author(s):  
James Michael Rini ◽  
Theo Hofmann ◽  
Jeremy P. Carver
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Cdna Clone ◽  
Edman Degradation ◽  
Pea Seeds ◽  
Pea Seed

The complete amino acid sequence of the alpha chains of both isolectins found in pea seeds has been determined using automated Edman degradation. We show that the alpha chains of these two proteins differ only at their C-termini: isolectin B is two amino acids longer than isolectin A. Furthermore, the alpha chains of both isolectins are shorter than would be predicted from the nucleotide sequence of a cDNA clone for pea lectin. We suggest, therefore, that these proteins arise from differential C-terminal processing. Amino acid composition data and C-terminal analysis show that the beta chains have also been processed at their C-termini, but in this case identical chains for both isolectins are produced.

scholarly journals Comparative studies of two types of bovine immunoglobulin G heavy chains

1968 ◽  
Vol 107 (4) ◽  
pp. 559-564 ◽  
Author(s):  
C. P. Milstein ◽  
A. Feinstein
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Immunoglobulin G ◽  
Comparative Studies ◽  
Cyanogen Bromide ◽  
Serum Immunoglobulin ◽  
Heavy Chains ◽  
Bovine Immunoglobulin

‘Fingerprints’ of bovine colostrum and serum immunoglobulin G1 heavy chains were extremely similar, but different from serum immunoglobin G2 heavy chains. Serum immunoglobulin G1 and immunoglobulin G2 heavy chains were treated with cyanogen bromide. The fractions from the C-terminal end of the heavy chains were isolated and the amino acid sequence of this fraction from immunoglobulin G2 was:His-Glx-Ala-Leu-His-Asx-His-Tyr-Met-Gln-Lys-Ser-Thr-Ser-Lys-Ser-Ala-GlyThe amino acid composition of this fraction from immunoglobulin G1 was the same except for the methionine, which in immunoglobulin G1 was replaced by threonine.

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
Keyword(s):  
Hong Kong ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Heavy Chain ◽  
Cyanogen Bromide ◽  
Edman Degradation ◽  
Amino Acid Residues ◽  
Core Peptide ◽  
Cyanogen Bromide Fragment

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.

Amino acid sequence of cyanogen bromide fragment CB3 of hog pepsin

1981 ◽  
Vol 46 (3) ◽  
pp. 655-666
Author(s):  
Ladislav Morávek ◽  
Vladimír Kostka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Methionine Residues ◽  
Cyanogen Bromide Fragment

On the basis of the knowlidge of thermolytic, chymotryptic and substilisin peptides the amino acid sequence was determined of cyanogen bromide fragment CB3 representing the region between methionine residues I and II of pepsin: Thr-Gly-Ile-Leu-Gly-Tyr-Asp-Thr-Val-Gln-Val-Gly-Gly-Ile-Ser-Asp-Thr-Asn-Gln-Ile-Phe-Gly-Leu-Ser-Glu-Thr-Glu-Pro-Gly-Ser-Phe-Leu-Tyr-Tyr-Ala-Pro-Phe-Asp-Gly-Ile-Leu-Gly-Leu-Ala-Tyr-Pro-Ser-Ile-Ser-Ala-Ser-Gly-Ala-Thr-Pro-Val-Phe-Asp-Asn-Leu-Trp-Asp-Gln-Gly-Leu-Val-Ser-Gln-Asp-Leu-Phe-Ser-Val-Tyr-Leu-Ser-Ser-Asn-Asp-Asp-Ser-Gly-Ser-Val-Val-Leu-Leu-Gly-Gly-Ile-Asp-Ser-Ser-Tyr-Tyr-Thr-Gly-Ser-Leu-Asn-Trp-Val-Pro-Val-Ser-Val-Glu-Gly-Tyr-Trp-Gln-Ile-Thr-Leu-Asp-Ser-Ile-Thr-Met.

Amino acid sequence of cyanogen bromide fragment CB5 of human hemopexin

1989 ◽  
Vol 54 (3) ◽  
pp. 803-810 ◽  
Author(s):  
Ivan Kluh ◽  
Ladislav Morávek ◽  
Manfred Pavlík
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Acid Hydrolysis ◽  
Cyanogen Bromide ◽  
Polypeptide Chain ◽  
Amino Acid Residues ◽  
Mild Acid Hydrolysis ◽  
Methionine Residue ◽  
Cyanogen Bromide Fragment ◽  
Mild Acid

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.

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