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N‐terminal amino acid sequences of precursor and mature forms of α‐1‐antitrypsin
Author(s) -
Gross Volker,
Kaiser Clemens,
Tran-Thi Thuy-Anh,
Schmelzer Elmon,
Witt Irene,
Plummer Thomas H.,
Heinrich Peter C.
Publication year - 1983
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(83)80069-6
Subject(s) - terminal (telecommunication) , chemistry , amino acid , biochemistry , amino terminal , peptide sequence , stereochemistry , computer science , gene , telecommunications
α‐1‐Antitrypsin is found in hepatocytes as a high‐mannose glycoprotein ( M r 49000), extracellularly as a complex‐type glycoprotein ( M r 54000). Deglycosylation of both forms with peptide: N‐glycosidase led to proteins of identical app. M r (41000). The sequence of 26 N‐terminal amino acids of rat α 1 ‐antitrypsin was determined. A high content of polar amino acids was found. The partially characterized presequence of in vitro synthesized α 1 ‐antitrypsin showed a cluster of hydrophobic amino acids. A pre‐peptide of 24 amino acids is proposed. There is no evidence for the existence of a propeptide.