Amino acid sequence studies on the α chain of human fibrinogen. Characterization of 11 cyanogen bromide fragments

Biochemistry ◽  
1977 ◽  
Vol 16 (8) ◽  
pp. 1703-1709 ◽  
Author(s):  
R. F. Doolittle ◽  
K. G. Cassman ◽  
B. A. Cottrell ◽  
S. J. Friezner ◽  
J. T. Hucko ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Human Fibrinogen ◽  
Α Chain

Preliminary report on the amino acid sequence of the α-chain of human fibrinogen

1979 ◽  
Vol 14 (4-5) ◽  
pp. 787-792 ◽  
Author(s):  
R.F. Doolittle ◽  
B.A. Cottrell ◽  
D. Strong ◽  
K.W.K. Watt
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Preliminary Report ◽  
Human Fibrinogen ◽  
Α Chain

scholarly journals On the Primary Structure of Human Fibrinogen

1977 ◽  
Author(s):  
A. Henschen ◽  
F. Lottspeich ◽  
E. Töpfer-Petersen ◽  
R. Warbinek
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Cyanogen Bromide ◽  
Attachment Site ◽  
Complete Sequence ◽  
Cleavage Sites ◽  
Amino Acid Residues ◽  
Human Fibrinogen ◽  
Β Chain

The aim of the present investigation is to elucidate the primary structure of human fibrinogen. Through the work of several laboratories including our own large parts of the structure are now known. Here will be reported the complete amino acid sequence of the γ-chain (409 residues). Furthermore, the carbohydrate linkage site in the β-chain and plasmin cleavage sites in the β- and γ-chains have been identified.The peptide chains were isolated by CM-cellulose chromatography following mercaptolysis and alkylation. The γ-chain was cleaved in a way to produce large fragments suitable for automatic sequencing, e. g. with cyanogen bromide or trypsin after citraconylation. The sequences of the isolated fragments allowed reconstruction of the complete sequence of the γ-chain.The carbohydrate linkage site in the β-chain could be isolated by affinity chromatography on concanavalin A-agarose following cleavage of the chain by trypsin or cyanogen bromide. The sequence of 21 amino acid residues around the carbohydrate attachment site was determined.The plasmin cleavage site giving rise to N-terminal glycine in the γ-chain D-fragment was identified. The amino acid sequence linking plasmic fragments E and D in the β-chain was determined.

Amino acid sequence of thermolysin. Isolation and characterization of the fragments obtained by cleavage with cyanogen bromide

Biochemistry ◽  
1972 ◽  
Vol 11 (13) ◽  
pp. 2427-2435 ◽  
Author(s):  
Koiti Titani ◽  
Mark A. Hermodson ◽  
Lowell H. Ericsson ◽  
Kenneth A. Walsh ◽  
Hans Neurath
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Isolation And Characterization

scholarly journals Amino Acid Sequence Studies on the γ-Chain of Human Fibrinogen

1977 ◽  
Author(s):  
H. Bouma ◽  
B. A. Cottrell ◽  
S. J. Friezner ◽  
T. Takagi ◽  
R. F. Doolittle
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Sequence Data ◽  
Structural Features ◽  
Tryptic Digestion ◽  
Cysteine Residues ◽  
Human Fibrinogen

The γ-chain of human fibrinogen contains 400±10 residues, eight of which are methionines. As such, we have isolated and characterized nine cyanogen bromide peptides. The alignment of these fragments was attained by the isolation of key overlap peptides derived from the tryptic digestion of citraconylated γ-chains and succinylated and aminoethylated γ-chains. In the latter case we synthesized a radioactive aminoethylating agent which was especially useful in isolating all the cysteine-containing peptides. The amino acid sequence of most of these fragments has been accomplished by a variety of procedures. In general, our results are in harmony with those recently reported by Henschen et al. (Hoppe-Seyler’s Z. Physiol. Chem., 357, 605, 1976), although some differences exist.The most interesting structural features revealed by the sequence data include significant homologies with the α- and β-chains, especially with regard to the arrangement of certain key cysteine residues. Thus, the sequence at residues γ 135–139 is Cys-Gln-Glu-Pro-Cys, in striking parallel with the sequence at residues γ 19–23, which is Cys-Pro-Thr-Thr-Cys. The occurrence of similar pentapeptide skeins in the α- and β-chains, in each case separated by about the same number of residues, has both structural and evolutionary connotations.

Amino acid sequence studies on the α chain of human fibrinogen. Covalent structure of the α-chain portion of fragment D

Biochemistry ◽  
1977 ◽  
Vol 16 (8) ◽  
pp. 1710-1715 ◽  
Author(s):  
R. F. Doolittle ◽  
K. G. Cassman ◽  
B. A. Cottrell ◽  
S. J. Friezner ◽  
T. Takagi
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Fibrinogen ◽  
Covalent Structure ◽  
Α Chain
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