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Tissue-specific Analogues of Erythrocyte Protein 4.1 Retain Functional Domains by Richard A. Anderson; Isabel Correas; Charles Mazzucco; J. David Castle; Vincent T. Marchesi is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Tissue-specific Analogues of Erythrocyte Protein 4.1 Retain Functional Domains about?

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).

Who reads Tissue-specific Analogues of Erythrocyte Protein 4.1 Retain Functional Domains?

Author

Richard A. Anderson; Isabel Correas; Charles Mazzucco; J. David Castle; Vincent T. Marchesi

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0730-2312)

Published

1988

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)