Skip to main content
NCBI home page
The Journal of Clinical Investigation logoLink to The Journal of Clinical Investigation
. 1976 Feb;57(2):398–407. doi: 10.1172/JCI108291

Spontaneous in vivo isomerization of bovine serum albumin as a determinant of its normal catabolism.

K Wallevik
PMCID: PMC436664  PMID: 1254725

Abstract

By combination of isoelectric focusing and immunoelectrophoresis of fresh bovine plasma it is shown that 10% of the albumin in plasma has isoionic points equal to the intramolecular SS-interchanged isomers of bovine serum albumin (BSA). It is also shown that (a) albumin with the isoionic point of SS-interchanged BSA is produced in the cow from radioiodinated BSA depleted from SS-interchanged albumin before injection and (b) purified radiolabeled SS-interchanged BSA can be converted in vivo to albumin with the native isoionic point. On this basis, it is proposed that SS-interchanged albumin in vivo is in postsynthetic equilibrium with the "native" albumin conformation. The SS-interchanged isomers purified either from commerical BSA or from BSA submitted to SH-SS interchange was, after radioiodination with 125I, compared metabolically with "native" albumin labeled with 131I in the same calf. Both species of SS-interchanged albumins have fast initial turnover rates but obtain a normal rate of degradation after the reversion to native albumin. If the isomers formed in vivo have the same properties as the ones present in commercial BSA, at least 50% of the physiological degradation of albumin can be accounted for by the 6-7 times faster catabolic rates of these isomers.

Full text

PDF
398

Images in this article

405Image
on p.405

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BENACERRAF B., BIOZZI G., HALPERN B. N., STIFFEL C., MOUTON D. Phagocytosis of heat-denatured human serum albumin labelled with 131I and its use as a means of investigating liver blood flow. Br J Exp Pathol. 1957 Feb;38(1):35–48. [PMC free article] [PubMed] [Google Scholar]
  2. Bocci V., Masti L., Pacini A., Viti A. Catabolism of native and denatured serum 131-I-proteins by polymorphonuclear leucocytes. Exp Cell Res. 1968 Sep;52(1):129–139. doi: 10.1016/0014-4827(68)90552-1. [DOI] [PubMed] [Google Scholar]
  3. Buys C. H., Elferink M. G., Bouma J. M., Gruber M., Nieuwenhuis P. Proteolysis of formaldehyde-treated albumin in Kupffer cells and its inhibition by suramin. J Reticuloendothel Soc. 1973 Aug;14(2):209–223. [PubMed] [Google Scholar]
  4. COHEN S., HOLLOWAY R. C., MATTHEWS C., MCFARLANE A. S. Distribution and elimination of 131 I- and 14C-labelled plasma proteins in the rabbit. Biochem J. 1956 Jan;62(1):143–154. doi: 10.1042/bj0620143. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Chen R. F. Removal of fatty acids from serum albumin by charcoal treatment. J Biol Chem. 1967 Jan 25;242(2):173–181. [PubMed] [Google Scholar]
  6. FREEMAN T. The biological behaviour of normal and denatured human plasma albumin. Clin Chim Acta. 1959 Nov;4:788–792. doi: 10.1016/0009-8981(59)90029-4. [DOI] [PubMed] [Google Scholar]
  7. GORDON A. H. The use of the isolated perfused liver to detect alterations to plasma proteins. Biochem J. 1957 Jun;66(2):255–264. doi: 10.1042/bj0660255. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. KATZ J., ROSENFELD S., SELLERS A. L. Role of the kidney in plasma albumin catabolism. Am J Physiol. 1960 Apr;198:814–818. doi: 10.1152/ajplegacy.1960.198.4.814. [DOI] [PubMed] [Google Scholar]
  9. KATZ J., ROSENFELD S., SELLERS A. L. Sites of plasma albumin catabolism in the rat. Am J Physiol. 1961 Jun;200:1301–1306. doi: 10.1152/ajplegacy.1961.200.6.1301. [DOI] [PubMed] [Google Scholar]
  10. KILLANDER J. SEPARATION OF HUMAN HEME- AND HEMOGLOBIN-BINDING PLASMA PROTEINS, CERULOPLASMIN AND ALBUMIN BY GEL FILTRATION. Biochim Biophys Acta. 1964 Oct 9;93:1–14. doi: 10.1016/0304-4165(64)90254-5. [DOI] [PubMed] [Google Scholar]
  11. Laurell C. B., Thulin E. Thiol-disulfide interchange in the binding of bence jones proteins to alpha-antitrypsin, prealbumin, and albumin. J Exp Med. 1975 Feb 1;141(2):453–465. doi: 10.1084/jem.141.2.453. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. MATTHEWS C. M. The theory of tracer experiments with 131I-labelled plasma proteins. Phys Med Biol. 1957 Jul;2(1):36–53. doi: 10.1088/0031-9155/2/1/305. [DOI] [PubMed] [Google Scholar]
  13. MCFARLANE A. S. Labelling of plasma proteins with radioactive iodine. Biochem J. 1956 Jan;62(1):135–143. doi: 10.1042/bj0620135. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. MEGO J. L., MCQUEEN J. D. THE UPTAKE AND DEGRADATION OF INJECTED LABELED PROTEINS BY MOUSE-LIVER PARTICLES. Biochim Biophys Acta. 1965 Apr 12;100:136–143. doi: 10.1016/0304-4165(65)90436-8. [DOI] [PubMed] [Google Scholar]
  15. McFARLANE A. S. The behavior of I 131-labeled plasma proteins in vivo. Ann N Y Acad Sci. 1957 Aug 30;70(1):19–25. doi: 10.1111/j.1749-6632.1957.tb35374.x. [DOI] [PubMed] [Google Scholar]
  16. Nikkel H. J., Foster J. F. A reversible sulfhydryl-catalyzed structural alteraction of bovine mercaptalbumin. Biochemistry. 1971 Nov 23;10(24):4479–4486. doi: 10.1021/bi00800a020. [DOI] [PubMed] [Google Scholar]
  17. Noel J. K., Hunter M. J. Bovine mercaptalbumin and non-mercaptalbumin monomers. Interconversions and structural differences. J Biol Chem. 1972 Nov 25;247(22):7391–7406. [PubMed] [Google Scholar]
  18. PEDERSEN K. O. Exclusion chromatography. Arch Biochem Biophys. 1962 Sep;Suppl 1:157–168. [PubMed] [Google Scholar]
  19. Parving H. H., Rossing N., Nielsen S. L., Lassen N. A. Increased transcapillary escape rate of albumin, IgG, and IgM after plasma volume expansion. Am J Physiol. 1974 Aug;227(2):245–250. doi: 10.1152/ajplegacy.1974.227.2.245. [DOI] [PubMed] [Google Scholar]
  20. Parving H. H., Rossing N. Simultaneous determination of the transcapillary escape rate of albumin and IgG in normal and long-term juvenile diabetic subjects. Scand J Clin Lab Invest. 1973 Nov;32(3):239–244. doi: 10.3109/00365517309082466. [DOI] [PubMed] [Google Scholar]
  21. RAYMOND S. ACRYLAMIDE GEL ELECTROPHORESIS. Ann N Y Acad Sci. 1964 Dec 28;121:350–365. doi: 10.1111/j.1749-6632.1964.tb14208.x. [DOI] [PubMed] [Google Scholar]
  22. Rhodin J., Nicole P., Zweifach B. 1973 Eugene M. Landis Award presentation to Silvio Baez. Microvasc Res. 1974 Jan;7(1):1–2. doi: 10.1016/0026-2862(74)90031-4. [DOI] [PubMed] [Google Scholar]
  23. Rossing N., Jensen H. Metabolic studies of different albumin preparations. Clin Sci. 1967 Feb;32(1):89–99. [PubMed] [Google Scholar]
  24. SOLOMON A. K. Equations for tracer experiments. J Clin Invest. 1949 Nov;28(6 Pt 1):1297–1307. doi: 10.1172/JCI102197. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. STERLING K. The turnover rate of serum albumin in man as measured by I131-tagged albumin. J Clin Invest. 1951 Nov;30(11):1228–1237. doi: 10.1172/JCI102542. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Smithies O. Disulfide-bond cleavage and formation in proteins. Science. 1965 Dec 17;150(3703):1595–1598. doi: 10.1126/science.150.3703.1595. [DOI] [PubMed] [Google Scholar]
  27. Stroupe S. D., Foster J. F. Further studies of the sulfhydryl-catalyzed isomerization of bovine mercaptalbumin. Biochemistry. 1973 Sep 25;12(20):3824–3830. doi: 10.1021/bi00744a005. [DOI] [PubMed] [Google Scholar]
  28. Svendsen P. J. Fused rocket immunoelectrophoresis. Scand J Immunol Suppl. 1973;1:69–70. doi: 10.1111/j.1365-3083.1973.tb03781.x. [DOI] [PubMed] [Google Scholar]
  29. TARVER H., ARMSTRONG F. B., DEBRO J. R., MARGEN S. Catabolism of plasma protein in the gut. Ann N Y Acad Sci. 1961 Aug 31;94:23–30. doi: 10.1111/j.1749-6632.1961.tb35529.x. [DOI] [PubMed] [Google Scholar]
  30. Wallevik K., Mouridsen H. T. Detection of metabolic denaturation of serum albumin by gel electrophoresis. Scand J Clin Lab Invest. 1973 Mar;31(2):225–230. doi: 10.3109/00365517309084314. [DOI] [PubMed] [Google Scholar]
  31. Wallevik K. SS-interchanged and oxidized isomers of bovine serum albumin separated by isoelectric focusing. Biochim Biophys Acta. 1976 Jan 20;420(1):42–56. doi: 10.1016/0005-2795(76)90343-3. [DOI] [PubMed] [Google Scholar]
  32. Wallevik K. Spontaneous denaturation as a possible initial step in the breakdown of serum albumin in vivo. Clin Sci Mol Med. 1973 Nov;45(5):665–675. doi: 10.1042/cs0450665. [DOI] [PubMed] [Google Scholar]
  33. Weeke B. Rocket immunoelectrophoresis. Scand J Immunol Suppl. 1973;1:37–46. doi: 10.1111/j.1365-3083.1973.tb03777.x. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Clinical Investigation are provided here courtesy of American Society for Clinical Investigation

RESOURCES