alpha-chymotrypsin and formic-acid

alpha-chymotrypsin has been researched along with formic-acid* in 2 studies

Other Studies

2 other study(ies) available for alpha-chymotrypsin and formic-acid

Article	Year
The amino acid sequence of pancreatic spasmolytic polypeptide. Biochimica et biophysica acta, 1985, Mar-01, Volume: 827, Issue:3 The sequence of porcine pancreatic spasmolytic polypeptide has been established by a variety of techniques including manual as well as automatic sequencing of fragments resulting from the cleavage of reduced and S-carboxymethylated pancreatic spasmolytic polypeptide with trypsin, chymotrypsin, clostripain, cyanogen bromide and formic acid. The N- and C-terminal sequences were established using pyroglutamate amino-peptidase and carboxypeptidase A, respectively. Pancreatic spasmolytic polypeptide contains 106 amino acid residues in a single chain with seven S-S bridges and a pyroglutamyl blocked N-terminal. The alignment of the sequences representing amino acids 14-49 and 63-98 shows pair-wise identical amino acid residues in 18 out of 36 positions, indicating that these two "domains" have been derived from a common gene. Topics: Amino Acid Sequence; Animals; Chymotrypsin; Cyanogen Bromide; Cysteine Endopeptidases; Endopeptidases; Formates; Intercellular Signaling Peptides and Proteins; Mucins; Muscle Proteins; Neuropeptides; Peptide Fragments; Peptides; Pyroglutamyl-Peptidase I; Swine; Trefoil Factor-2; Trefoil Factor-3; Trypsin	1985
Hemocyanins in Spiders, XVIII. Complete amino-acid sequence of subunit e from Eurypelma californicum hemocyanin. Hoppe-Seyler's Zeitschrift fur physiologische Chemie, 1983, Volume: 364, Issue:10 The complete amino-acid sequence of subunit e of the hemocyanin from the tarantula, Eurypelma californicum, was determined by a combination of manual and automated methods. By limited proteolysis with chymotrypsin, two large fragments (e-CHn 29 and e-CHn 42) were obtained. The large peptides were further cleaved with cyanogen bromide, trypsin (with and without prior blocking of lysine residues), chymotrypsin, Staphylococcus aureus proteinase, Astacus fluviatilis proteinase, or 25% formic acid. The complete chain comprises 621 residues. A remarkable feature of the sequence is a hexapeptide -His-His-Trp-His-Trp-His- which is believed to take part in the binding of copper. Topics: Amino Acid Sequence; Animals; Chemical Phenomena; Chemistry; Chymotrypsin; Cyanogen Bromide; Endopeptidases; Formates; Hemocyanins; Hydrolysis; Peptide Fragments; Serine Endopeptidases; Spiders; Trypsin	1983

Article

Year

The amino acid sequence of pancreatic spasmolytic polypeptide.

Biochimica et biophysica acta, 1985, Mar-01, Volume: 827, Issue:3

The sequence of porcine pancreatic spasmolytic polypeptide has been established by a variety of techniques including manual as well as automatic sequencing of fragments resulting from the cleavage of reduced and S-carboxymethylated pancreatic spasmolytic polypeptide with trypsin, chymotrypsin, clostripain, cyanogen bromide and formic acid. The N- and C-terminal sequences were established using pyroglutamate amino-peptidase and carboxypeptidase A, respectively. Pancreatic spasmolytic polypeptide contains 106 amino acid residues in a single chain with seven S-S bridges and a pyroglutamyl blocked N-terminal. The alignment of the sequences representing amino acids 14-49 and 63-98 shows pair-wise identical amino acid residues in 18 out of 36 positions, indicating that these two "domains" have been derived from a common gene.

Topics: Amino Acid Sequence; Animals; Chymotrypsin; Cyanogen Bromide; Cysteine Endopeptidases; Endopeptidases; Formates; Intercellular Signaling Peptides and Proteins; Mucins; Muscle Proteins; Neuropeptides; Peptide Fragments; Peptides; Pyroglutamyl-Peptidase I; Swine; Trefoil Factor-2; Trefoil Factor-3; Trypsin

1985

Hemocyanins in Spiders, XVIII. Complete amino-acid sequence of subunit e from Eurypelma californicum hemocyanin.

Hoppe-Seyler's Zeitschrift fur physiologische Chemie, 1983, Volume: 364, Issue:10

The complete amino-acid sequence of subunit e of the hemocyanin from the tarantula, Eurypelma californicum, was determined by a combination of manual and automated methods. By limited proteolysis with chymotrypsin, two large fragments (e-CHn 29 and e-CHn 42) were obtained. The large peptides were further cleaved with cyanogen bromide, trypsin (with and without prior blocking of lysine residues), chymotrypsin, Staphylococcus aureus proteinase, Astacus fluviatilis proteinase, or 25% formic acid. The complete chain comprises 621 residues. A remarkable feature of the sequence is a hexapeptide -His-His-Trp-His-Trp-His- which is believed to take part in the binding of copper.

Topics: Amino Acid Sequence; Animals; Chemical Phenomena; Chemistry; Chymotrypsin; Cyanogen Bromide; Endopeptidases; Formates; Hemocyanins; Hydrolysis; Peptide Fragments; Serine Endopeptidases; Spiders; Trypsin

1983