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Isolation, characterization and partial sequencing of Pregnancy Associated Mouse Protein PAMP1 identifies it as a novel female specific protein, unrelated to the α‐2‐macroglobulin family of proteinase inhibitors
Author(s) -
Van Leuven Fred,
Torrekens Sophie,
Van den Berghe Herman
Publication year - 1993
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(93)81573-i
Subject(s) - cyanogen bromide , peptide sequence , macroglobulin , protein family , biology , molecular mass , protein sequencing , protein primary structure , protein subunit , biochemistry , microbiology and biotechnology , enzyme , gene
Pregnancy Associated Mouse Protein 1 (PAMP1) was isolated from plasma of female mice. An antiserum raised against the purified protein confirmed its immunochemical identity with the originally described PAMP1. Pregnant females were observed to have plasma levels of PAMP1 that are increased two‐fold at day 10–13 of gestation relative to non‐pregnant females, while male mouse plasma did not contain PAMP1. The purified protein displayed an apparent subunit molecular mass of 70 kDa, irrespective of cystine reduction. The native molecular mass, estimated by gel‐filtration, was about 140 kDa, indicating that PAMP1 is circulating as a non‐covalent homodimer. The amino‐terminal sequence of the intact protein and the internal sequences of four cyanogen bromide fragments demonstrated that this protein is not related to any known member of the α‐2‐macroglobulin family nor to any protein in the sequence databases. The physicochemical and the sequence data thus establish this protein as a novel, female‐specific protein, but unrelated to the Macroglobulin proteinase inhibitor family.