Isolation and characterization of a cDNA clone coding for the calcium-binding subunit of calcineurin from bovine brain: An identical amino acid sequence to the human protein

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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Isolation and characterization of reptilian insulin: Partial amino acid sequence of rattlesnake (Crotalus atrox) insulin

General and Comparative Endocrinology ◽

10.1016/0016-6480(76)90184-2 ◽

1976 ◽

Vol 28 (3) ◽

pp. 320-333 ◽

Cited By ~ 25

Author(s):

Joe R. Kimmel ◽

Michael J. Maher ◽

H.Gail Pollock ◽

William H. Vensel

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Partial Amino Acid Sequence ◽

Crotalus Atrox ◽

Isolation And Characterization

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Characterization of the sulfated glycopeptide of chicken pepsinogen

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19820709 ◽

1982 ◽

Vol 47 (2) ◽

pp. 709-718 ◽

Cited By ~ 6

Author(s):

Miroslav Baudyš ◽

Vladimír Kostka ◽

Karel Grüner ◽

Jan Pohl

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Protein Molecule ◽

Amino Acid Residues ◽

Terminal Sequence ◽

Sugar Moiety ◽

Pepsinogen A ◽

Identical Amino Acid Sequence ◽

High Voltage Electrophoresis

S-sulfonated chicken pepsinogen was digested with TPCK-trypsin; large tryptic peptides, separated on Sephadex G-25 fine, were subjected to additional cleavage with α-chymotrypsin. The hold-up fraction of the chymotryptic digest from the Sephadex G-25 column, was resolved by high voltage electrophoresis. The three most acidic zones contained glycopeptides of identical amino acid sequence Val-Ser-Thr-Asn-Glu-Thr-Val-Tyr, yet differed in the composition of the sugar moiety. These glycopeptides, moreover, bear different numbers of sulfate groups which enabled the resolution of the peptides. The most acidic glycopeptide contains 7 glucosamine residues, 3 mannose residues and 5 sulfate groups, the second one 6 glucosamine residues, 3 mannose residues and 4 sulfate groups and the slowest, minority glycopeptide, 5 glucosamine residues, 2 mannose residues and 2 sulfate groups. The entire sugar moiety is attached to one of the chain viaasparagine. In other experiments the glycopeptides were also isolated from the thermolytic digest of chicken pepsin; their C-terminal sequence was shorter by two amino acid residues. The tentative assignment of the glycopeptides to the amino acid sequence of pepsinogen resulted from the analysis of the limited tryptic digest of the whole protein molecule. Chicken pepsinogen is glycosylated at the site of the chain occupied by a phosphoserine residue in hog pepsinogen A.

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