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Binding and endocytosis of alpha 2-macroglobulin-plasmin complexes.

Publication ,  Journal Article
Ney, KA; Gidwitz, S; Pizzo, SV
Published in: Biochemistry
August 13, 1985

The clearance of 125I-labeled alpha 2-macroglobulin-plasmin complexes (125I-alpha 2M-PM) from mouse circulation is slower than that of 125I-labeled alpha 2M-methylamine complexes (125I-alpha 2M-CH3NH2). In addition, clearance of 125I-alpha 2M-PM is biphasic, but that of 125I-alpha 2M-CH3NH2 follows simple first-order kinetics. Treatment of alpha 2M-PM with trypsin yields a complex that clears like alpha 2M-CH3NH2. Complexes of alpha 2M with Val442-plasmin (alpha 2M-Val442-PM) were prepared; alpha 2M-Val442-PM has a stoichiometry of 2 mol of Val442-PM to 1 mol of alpha 2M and also clears like alpha 2M-CH3NH2. In vitro 4 degrees C binding inhibition studies with mouse peritoneal macrophages show that alpha 2M-CH3NH2, alpha 2M-PM, trypsin-treated alpha 2M-PM, and alpha 2M-Val442-PM bind with the same affinity, apparent Kd = 0.4 nM. The binding isotherms at 4 degrees C are the same for 125I-alpha 2M-CH3NH2, 125I-alpha 2M-PM, and 125I-trypsin-treated alpha 2M-PM in both mouse peritoneal macrophages and 3T3-L1 fibroblasts. The Scatchard plots for the binding isotherms in macrophages were curved; those in 3T3-L1 fibroblasts were linear with an apparent Kd of 0.48 nM and a receptor activity of 140 fmol/mg of cell protein for alpha 2M-CH3NH2, an apparent Kd of 0.29 nM and a receptor activity of 110 fmol/mg of cell protein for alpha 2M-PM, and an apparent Kd of 0.35 nM and a receptor activity of 210 fmol/mg of cell protein for trypsin-treated alpha 2M-PM.(ABSTRACT TRUNCATED AT 250 WORDS)

Duke Scholars

Published In

Biochemistry

DOI

ISSN

0006-2960

Publication Date

August 13, 1985

Volume

24

Issue

17

Start / End Page

4586 / 4592

Location

United States

Related Subject Headings

  • alpha-Macroglobulins
  • Trypsin
  • Protein Binding
  • Plasminogen
  • Mice
  • Macromolecular Substances
  • Kinetics
  • Humans
  • Fibroblasts
  • Fibrinolysin
 

Citation

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MLA
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Ney, K. A., Gidwitz, S., & Pizzo, S. V. (1985). Binding and endocytosis of alpha 2-macroglobulin-plasmin complexes. Biochemistry, 24(17), 4586–4592. https://doi.org/10.1021/bi00338a016
Ney, K. A., S. Gidwitz, and S. V. Pizzo. “Binding and endocytosis of alpha 2-macroglobulin-plasmin complexes.Biochemistry 24, no. 17 (August 13, 1985): 4586–92. https://doi.org/10.1021/bi00338a016.
Ney KA, Gidwitz S, Pizzo SV. Binding and endocytosis of alpha 2-macroglobulin-plasmin complexes. Biochemistry. 1985 Aug 13;24(17):4586–92.
Ney, K. A., et al. “Binding and endocytosis of alpha 2-macroglobulin-plasmin complexes.Biochemistry, vol. 24, no. 17, Aug. 1985, pp. 4586–92. Pubmed, doi:10.1021/bi00338a016.
Ney KA, Gidwitz S, Pizzo SV. Binding and endocytosis of alpha 2-macroglobulin-plasmin complexes. Biochemistry. 1985 Aug 13;24(17):4586–4592.
Journal cover image

Published In

Biochemistry

DOI

ISSN

0006-2960

Publication Date

August 13, 1985

Volume

24

Issue

17

Start / End Page

4586 / 4592

Location

United States

Related Subject Headings

  • alpha-Macroglobulins
  • Trypsin
  • Protein Binding
  • Plasminogen
  • Mice
  • Macromolecular Substances
  • Kinetics
  • Humans
  • Fibroblasts
  • Fibrinolysin