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Journal of Biochemistry 2005 138(5):527-537; doi:10.1093/jb/mvi162
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© 2005 The Japanese Biochemical Society

Regular Paper

The Properties of Rabbit {alpha}1-Macroglobulin upon Activation Are Distinct from Those of Rabbit and Human {alpha}2-Macroglobulins

Agnieszka Banbula*, Lara S. Chang*, Wayne F. Beyer*, Charu L. Bohra, George J. Cianciolo and Salvatore V. Pizzo{dagger}

Department of Pathology, Box 3712, Duke University Medical Center, Durham, NC 27710, USA

{dagger} To whom correspondence should be addressed. Phone: +1-919-684-3528, Fax: +1-919-684-8689, E-mail: pizzo001{at}mc.duke.edu

We have characterized native and activated forms of rabbit {alpha}1M and compared them to rabbit and human {alpha}2M. Similar to human {alpha}2M, rabbit {alpha}1M is a tetramer associated via disulfide bonds and non-covalent interactions that exhibits autolysis into two fragments when heated. Like human {alpha}2M, rabbit {alpha}1M is cleaved by trypsin at one site; however, rabbit {alpha}1M shares characteristics with rabbit {alpha}2M that are different from the properties of human {alpha}2M. Amine or trypsin treatment of rabbit {alpha}-macroglobulins does not result in a significant conformational change or cleavage of four thiolester bonds. Full thiolester cleavage is only observed for rabbit {alpha}1M after exposure to both trypsin and a small amine. Additionally, amine-treated rabbit {alpha}-macroglobulins retain trypsin inhibitory potential and do not fully shield bound proteinases. Methylamine and trypsin treatment of rabbit {alpha}1M results in two dissimilar conformations that display differing exposure of the receptor-recognition site. While ammonia- and methylamine-modified rabbit {alpha}1M bind to macrophages with similar affinity to that of human {alpha}2M, trypsin-treated rabbit {alpha}1M exhibits dramatically lower affinity. This suggests that rabbit {alpha}1M may not play the same proteinase-inhibiting physiological role as human {alpha}2M.

* These authors contributed equally.


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