Premium
α 2 ‐Macroglobulin bait region integrity
Author(s) -
Gettins Peter G.W.,
Beechem Joseph M.,
Crews Brenda C.
Publication year - 1993
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(93)81086-f
Subject(s) - cleavage (geology) , chemistry , cysteine , alpha 2 macroglobulin , fluorophore , alpha (finance) , methylamine , covalent bond , fluorescence , biochemistry , macroglobulin , biology , enzyme , organic chemistry , physics , medicine , paleontology , construct validity , nursing , quantum mechanics , fracture (geology) , patient satisfaction
To determine whether integrity of the bait region affects the structure of the remainder of human α 2 ‐macroglobulin (α 2 M), we have determined the separation between cysteine residues in a methylamine‐reacted fast‐form of α 2 M. From reduction in fluorescence intensity of covalently‐bound donor fluorophore caused by proximity to an acceptor, a separation of 35 ± 8 Å was calculated, which is identical to a previously determined value for proteinase‐treated fast‐form α 2 M. This indicates that although bait region cleavage is the physiological route to conformational change in α 2 M, bait region integrity per se does not significantly affect the structure of fast‐form α 2 M.