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Monomeric pituitary growth hormone and prolactin variants in man characterized by immunoperoxidase electrophoresis
Author(s) -
Meuris Sylvain,
Svoboda Michal,
Vilamala Maria,
Christophe Jean,
Robyn Claude
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)80885-0
Subject(s) - immunoperoxidase , prolactin , microbiology and biotechnology , peptide , pituitary gland , staining , monomer , biology , endocrinology , gel electrophoresis , chemistry , medicine , biochemistry , antibody , hormone , monoclonal antibody , immunology , genetics , organic chemistry , polymer
Immunoperoxidase electrophoresis, combining SDS‐ME‐PAGE and the ‘double bridge’ immunoperoxidase staining was applied to crude human pituitary homogenates. With anti‐hGH and anti‐hPL sera, 4 hGH‐related monomers were characterized: a M r 22 000 peptide corresponding to hGH; a M r 20 000 peptide corresponding to the known hGH variant and two unknown hGH variants ( M r 65 000 and M r 75 000). With anti‐ovine, rat and human PRL sera, 4 PRL‐related monomers were immunostained: one comigrated with purified hPRL ( M r 25 000), and 3 were unknown ( M r 29 000; M r 45 000; M r 16 000).