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Tissue‐specific analogues of erythrocyte protein 4.1 retain functional domains
Author(s) -
Anderson Richard A.,
Correas Isabel,
Mazzucco Charles,
Castle J. David,
Marchesi Vincent T.
Publication year - 1988
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240370303
Subject(s) - spectrin , gene isoform , epitope , biochemistry , cleavage (geology) , immunoprecipitation , cysteine , peptide , microbiology and biotechnology , molecular mass , blot , antibody , peptide sequence , chemistry , biology , cell , gene , cytoskeleton , enzyme , paleontology , fracture (geology) , immunology
Analogues of the human erythroid membrane skeletal component protein 4.1 have been identified in perfused rat tissues and human T and B lymphocyte cell lines, olyclonal antibodies were used which are specific for all domains of protein 4.1, the spectrin‐actin‐promoting 8‐Kd peptide, the membrane‐binding 30‐Kd domain, and the 50‐Kd domain. Antibody reactivity, by Western blotting of tissue homogenates, shows reactivity with proteins varying in molecular weight from 175 Kd to 30 Kd. Further, these protein 4.1 analogues appear to be expressed in a tissue‐specific fashion. Of the analogues detected there appear to be at least three classes: analogues containing all erythroid protein 4.1 domains, analogues containing all domains but with modified antigenic epitopes, and analogues containing only some domains. Chemical cleavage at cysteine linkages indicates that in analogues containing the 30‐Kd region the location of cysteine is highly conserved. This datum suggests that in nonerythroid 4.1 isoforms of higher molecular weight the additional protein mass is added to the amino terminal end (30 Kd end).