Amino acid sequence studies on the α chain of human fibrinogen. Isolation and characterization of two linked α-chain cyanogen bromide fragments from fully cross-linked fibrin

Biochemistry ◽  
1977 ◽  
Vol 16 (8) ◽  
pp. 1715-1719 ◽  
Author(s):  
R. F. Doolittle ◽  
K. G. Cassman ◽  
B. A. Cottrell ◽  
S. J. Friezner
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Human Fibrinogen ◽  
Isolation And Characterization ◽  
Α Chain

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

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

Amino acid sequence of penicillopepsin. III. Isolation and characterization of amino terminal, tryptic, and tryptophanyl peptides

1976 ◽  
Vol 54 (10) ◽  
pp. 895-901
Author(s):  
C. Ian Harris ◽  
Leticia Rao ◽  
Paul Shutsa ◽  
Alexander Kurosky ◽  
Theo Hofmann
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Amino Acid Sequences ◽  
Affinity Column ◽  
Amino Terminal ◽  
Tryptic Digest ◽  
The Third ◽  
Isolation And Characterization

The amino acid sequences of peptides isolated from a tryptic digest of penicillopepsin (EC 3.4.23.7), a subtilisin (EC 3.4.21.14) digest of maleylated penicillopepsin, and a chymotryptic digest of penicillopepsin modified with dinitrophenylsulfenyl (DNPS) chloride have been determined. The first two digests identified four of the five lysyl residues of the enzyme as well as the N-terminal peptide. The third digest provided overlaps at three of the tryptophanyl residues. The DNPS-tryptophan peptides were isolated on an affinity column prepared by coupling dinitrophenyl antibody raised in sheep to cyanogen bromide-activated Sepharose.

Amino acid sequence of penicillopepsin. I. Isolation and characterization of the chymotryptic peptides

1976 ◽  
Vol 54 (10) ◽  
pp. 872-884 ◽  
Author(s):  
Alexander Kurosky ◽  
Theo Hofmann
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Acid Protease ◽  
Terminal Region ◽  
Isolation And Characterization

The amino acid sequences of 48 peptides obtained from a chymotryptic digest of the mould acid protease, penicillopepsin (EC 3.4.23.7), have been determined. These peptides established the sequences of 26 unique fragments of up to 28 residues in length. The 28-residue fragment was identified as the N-terminal region. The C-terminal region is represented by a 13-residue fragment. The amino acids contained in these fragments account for some 85% of the residues of the enzyme.

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