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Bovine α 2 ‐antiplasmin N‐Terminal and reactive site sequence
Author(s) -
Christensen Søren,
Sottrup-Jensen Lars
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81419-m
Subject(s) - amino acid residue , chemistry , residue (chemistry) , peptide sequence , sequence (biology) , homologous chromosome , biochemistry , microbiology and biotechnology , stereochemistry , biology , gene
Bovine α 2 ‐antiplasmin (α 2 AP) has been purified and partially characterized. The amino acid composition is very similar to that of human α 2 AP, and the N‐terminal (23 residues determined) and reactive site loop sequences (42 residues determined) are highly homologous to those of the human protein. Compared with human α 2 AP, bovine α 2 AP has an 18‐residue N‐terminal extension, homologous with part of the pre‐sequence of human α 2 AP. A re‐investigation of the N‐terminal sequence of freshly prepared human α 2 AP reveals a new form extended by 12 residues.