α2‐Macroglobulin bait region integrity

FEBS Letters

Beechem, Joseph M.²  Gettins, Peter G.W.¹  Crews, Brenda C.¹ 

[1] Department of Biochemistry and Center in Molecular Toxicology Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA;Department of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA

关键词: α2-Macroglobulin;    Bait region;    Fluorescence resonance energy transfer;    α2M;    α2-macroglobulin;    I-form α2M;    intermediate form α2M;    PAGE;    polyacrylamide gel electrophoresis;    5-IAF;    5-iodoacetamidofluorescein;   

DOI  :  10.1016/0014-5793(93)81086-F

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

To determine whether integrity of the bait region affects the structure of the remainder of human α₂-macroglobulin (α₂M), we have determined the separation between cysteine residues in a methylamine-reacted fast-form of α₂ 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 α₂M. This indicates that although bait region cleavage is the physiological route to conformational change in α₂M, bait region integrity per se does not significantly affect the structure of fast-form α₂M.

【 授权许可】

Unknown