Thio reduction of human 2 -macroglobulin. The subunit structure - PubMed (original) (raw)
Thio reduction of human 2 -macroglobulin. The subunit structure
J M Jones et al. Biochem J. 1972 Mar.
Abstract
1. Human alpha(2)-macroglobulin was prepared from a fraction obtained during the large-scale separation of normal human plasma proteins for clinical use. 2. Sedimentation-equilibrium measurements indicated a molecular weight of 725000. A value of 18.1S was obtained for s(0) (20,w). 3. The dissociation that occurs in the pH range 4.5-2.5 and in the region of neutrality in urea-containing solutions is consistent with a dimeric structure of the molecule. 4. The effects of the thiol reagents mercaptoethanol, mercaptoethylamine and N-acetylcysteine were investigated over a range of experimental conditions. Distinct components having sedimentation coefficients of 15, 12 and 8.5S were identified. 5. Conditions were found under which limited reduction with thiol liberated a subunit with a molecular weight approximately one-quarter of that of the intact molecule. This subunit retains the serological specificity of the whole molecule.
Similar articles
- Kinetics and thermodynamic study on the chemical reduction of macroimmunoglobulins.
Utzig E, Rialdi G. Utzig E, et al. Mol Immunol. 1990 Apr;27(4):343-50. doi: 10.1016/0161-5890(90)90047-4. Mol Immunol. 1990. PMID: 2359412 - Subunit structure and dissociation of Callinectes sapidus hemocyanin.
Herskovits TT, Erhunmwunsee LJ, San George RC, Herp A. Herskovits TT, et al. Biochim Biophys Acta. 1981 Jan 30;667(1):44-58. doi: 10.1016/0005-2795(81)90065-9. Biochim Biophys Acta. 1981. PMID: 7213799 - The mitotic apparatus. Physical chemical characterization of the 22S protein component and its subunits.
Stephens RE. Stephens RE. J Cell Biol. 1967 Feb;32(2):255-75. doi: 10.1083/jcb.32.2.255. J Cell Biol. 1967. PMID: 10976220 Free PMC article. - [Dissociation of Penicillium vitale catalase under the effect of urea and acid pH].
Mironenko NI, Protvin DD, Degtiar RG, Guliĭ MF. Mironenko NI, et al. Ukr Biokhim Zh. 1977 May-Jun;49(3):94-8. Ukr Biokhim Zh. 1977. PMID: 18833 Ukrainian. - Physical properties and subunit structure of L-asparaginase isolated from Erwinia carotovora.
Cammack KA, Marlborough DI, Miller DS. Cammack KA, et al. Biochem J. 1972 Jan;126(2):361-79. doi: 10.1042/bj1260361. Biochem J. 1972. PMID: 4561025 Free PMC article.
Cited by
- Frozen fresh blood plasma preserves the functionality of native human α2-macroglobulin.
Mendes SR, Gomis-Rüth FX, Goulas T. Mendes SR, et al. Sci Rep. 2023 Mar 20;13(1):4579. doi: 10.1038/s41598-023-31800-8. Sci Rep. 2023. PMID: 36941303 Free PMC article. - Covalent binding of proteinases in their reaction with alpha 2-macroglobulin.
Salvesen GS, Barrett AJ. Salvesen GS, et al. Biochem J. 1980 Jun 1;187(3):695-701. doi: 10.1042/bj1870695. Biochem J. 1980. PMID: 6204637 Free PMC article. - Stoichiometry of reactions of alpha 2-macroglobulin with trypsin and chymotrypsin.
Björk I, Larsson LJ, Lindblom T, Raub E. Björk I, et al. Biochem J. 1984 Jan 1;217(1):303-8. doi: 10.1042/bj2170303. Biochem J. 1984. PMID: 6199019 Free PMC article. - Complex-formation and inhibition of urokinase by blood plasma proteins.
Waller EK, Schleuning WD, Reich E. Waller EK, et al. Biochem J. 1983 Oct 1;215(1):123-31. doi: 10.1042/bj2150123. Biochem J. 1983. PMID: 6194790 Free PMC article. - Differential scanning calorimetry of alpha 2-macroglobulin and alpha 2-macroglobulin-proteinase complexes.
Chlebowski JF, Williams K. Chlebowski JF, et al. Biochem J. 1983 Mar 1;209(3):725-30. doi: 10.1042/bj2090725. Biochem J. 1983. PMID: 6191752 Free PMC article.
References
- Nature. 1967 Jun 17;214(5094):1226-7 - PubMed
- Biochem J. 1955 Aug;60(4):671-83 - PubMed
- Nature. 1967 Nov 4;216(5114):500-1 - PubMed
- Ann N Y Acad Sci. 1964 Dec 28;121:404-27 - PubMed
- Proc Natl Acad Sci U S A. 1956 Sep;42(9):596-603 - PubMed
MeSH terms
Substances
LinkOut - more resources
Full Text Sources