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Probing the stability of native and activated forms of alpha2-macroglobulin.

Publication ,  Journal Article
Kaczowka, SJ; Madding, LS; Epting, KL; Kelly, RM; Cianciolo, GJ; Pizzo, SV
Published in: Int J Biol Macromol
January 1, 2008

alpha2-Macroglobulin (alpha2M) is a 718 kDa homotetrameric proteinase inhibitor which undergoes a large conformational change upon activation. This conformational change can occur either by proteolytic attack on an approximately 40 amino acid stretch, the bait region, which results in the rupture of the four thioester bonds in alpha2M, or by direct nucleophilic attack on these thioesters by primary amines. Amine activation circumvents both bait region cleavage and protein incorporation, which occurs by proteolytic activation. These different activation methods allow for examination of the roles bait region cleavage and thioester rupture play in alpha2M stability. Differential scanning calorimetry and urea gel electrophoresis demonstrate that both bait region cleavage and covalent incorporation of protein ligands in the thioester pocket play critical roles in the stability of alpha2M complexes.

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Published In

Int J Biol Macromol

DOI

ISSN

0141-8130

Publication Date

January 1, 2008

Volume

42

Issue

1

Start / End Page

62 / 67

Location

Netherlands

Related Subject Headings

  • alpha-Macroglobulins
  • Transition Temperature
  • Protein Conformation
  • Polymers
  • Peptide Hydrolases
  • Molecular Sequence Data
  • Ligands
  • Humans
  • Hot Temperature
  • Animals
 

Citation

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Kaczowka, S. J., Madding, L. S., Epting, K. L., Kelly, R. M., Cianciolo, G. J., & Pizzo, S. V. (2008). Probing the stability of native and activated forms of alpha2-macroglobulin. Int J Biol Macromol, 42(1), 62–67. https://doi.org/10.1016/j.ijbiomac.2007.09.019
Kaczowka, Steven J., Lara S. Madding, Kevin L. Epting, Robert M. Kelly, George J. Cianciolo, and Salvatore V. Pizzo. “Probing the stability of native and activated forms of alpha2-macroglobulin.Int J Biol Macromol 42, no. 1 (January 1, 2008): 62–67. https://doi.org/10.1016/j.ijbiomac.2007.09.019.
Kaczowka SJ, Madding LS, Epting KL, Kelly RM, Cianciolo GJ, Pizzo SV. Probing the stability of native and activated forms of alpha2-macroglobulin. Int J Biol Macromol. 2008 Jan 1;42(1):62–7.
Kaczowka, Steven J., et al. “Probing the stability of native and activated forms of alpha2-macroglobulin.Int J Biol Macromol, vol. 42, no. 1, Jan. 2008, pp. 62–67. Pubmed, doi:10.1016/j.ijbiomac.2007.09.019.
Kaczowka SJ, Madding LS, Epting KL, Kelly RM, Cianciolo GJ, Pizzo SV. Probing the stability of native and activated forms of alpha2-macroglobulin. Int J Biol Macromol. 2008 Jan 1;42(1):62–67.
Journal cover image

Published In

Int J Biol Macromol

DOI

ISSN

0141-8130

Publication Date

January 1, 2008

Volume

42

Issue

1

Start / End Page

62 / 67

Location

Netherlands

Related Subject Headings

  • alpha-Macroglobulins
  • Transition Temperature
  • Protein Conformation
  • Polymers
  • Peptide Hydrolases
  • Molecular Sequence Data
  • Ligands
  • Humans
  • Hot Temperature
  • Animals