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Molecular species of epidermal growth factor carrying immunosuppressive activity
Author(s) -
Koch J. H.,
Fifis T.,
Bender V. J.,
Moss B. A.
Publication year - 1984
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.240250105
Subject(s) - epidermal growth factor , asparagine , biology , biological activity , amino acid , microbiology and biotechnology , biochemistry , chemistry , receptor , in vitro
The suppression of antibody formation to sheep red cells in mice by partially purified fractions of mouse submaxillary gland [7] was shown to be caused by epidermal growth factor (EGF). Purification of EGF by the method of Savage and Cohen [11] resolved three components referred to as EGF a , EGF b , and EGF c. All three induced premature eye opening in neonatal mice, but only EGF a (identified as EGF 1‐53 ) had full immunosuppressive activity. EGF c was shown by micropeptide mapping of chymotryptic and thermolytic digests and aminoterminal analysis to differ from EGF a only by the presence of β‐aspartyl instead of an asparaginyl residue. EGF b differed from EGF a in that it lacked the N‐terminal asparagine. EGF shortened enzymatically at its carboxy terminal by two or five amino acids did not have any immunosuppressive activity. These findings‐suggest that, in contrast to some other biological effects of EGF, intact amino and carboxy terminals are required for the expression of immunosuppressive activity.