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The serum proteome of Equus caballus
Author(s) -
Miller Ingrid,
Friedlein Arno,
Tsangaris George,
Maris Antony,
Fountoulakis Michael,
Gemeiner Manfred
Publication year - 2004
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200400846
Subject(s) - proteome , haptoglobin , chemistry , equus , blood proteins , matrix assisted laser desorption/ionization , transthyretin , proteomics , mass spectrometry , gel electrophoresis , microbiology and biotechnology , albumin , two dimensional gel electrophoresis , tandem mass spectrometry , chromatography , biology , biochemistry , gene , immunology , desorption , zoology , organic chemistry , adsorption , endocrinology
We constructed a reference two‐dimensional protein map for horse ( Equus caballus ) serum. The serum proteins were separated by two‐dimensional electrophoresis (2‐DE); 29 different gene products were identified. Proteins represented by 25 spots/spot groups were identified by tandem nanoelectrospray mass spectrometry (MS), four by matrix‐assisted laser desorption ionization time‐of‐flight (TOF) MS and one was sequenced by TOF‐TOF technology. The identities of four proteins were deduced by similarity to the human plasma protein database. In selected cases, i.e. the immunoglobulins, immunoblotting with specific antibodies provided additional information about the respective proteins. Albumin was detected as the full‐length protein and as fragments of various sizes. Spots representing products of different mass and charge were also detected for α 1 ‐antitrypsin, haptoglobin and transthyretin. Thus, despite the fact that the Equus caballus genome is incompletely characterizated, we were able to identify almost all moderate to high abundance proteins stained in the serum 2‐DE pattern.