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. 1973 Aug;134(4):1083–1091. doi: 10.1042/bj1341083

Biosynthesis of serum albumin in rat liver. Evidence for the existence of `proalbumin'

J D Judah 1, Margaret Gamble 1, J H Steadman 1
PMCID: PMC1177917  PMID: 4762753

Abstract

1. A protein(s) of rat liver (precipitated from soluble extracts of the microsomal fraction by anti-albumin) yields albumin after limited hydrolysis by trypsin. 2. Evidence that the product of limited tryptic hydrolysis is albumin, is based upon ion-exchange chromatography, electrofocusing and peptide `mapping'. 3. The albumin `precursor' is recognized by anti-albumin and is apparently not distinguished from albumin by anti-albumin. 4. A small peptide is liberated from the presumptive albumin precursor during limited tryptic hydrolysis. This peptide is labelled by arginine, but not by leucine, lysine or methionine. 5. These results support our previous suggestion based on kinetic evidence that the albumin-like protein(s), in the anti-albumin precipitate from rat liver, is an albumin precursor.

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Selected References

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  1. 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]
  2. DEBRO J. R., TARVER H., KORNER A. The determination of serum albumin and globulin by a new method. J Lab Clin Med. 1957 Nov;50(5):728–732. [PubMed] [Google Scholar]
  3. GORDON A. H., HUMPHREY J. H. Measurement of intracellular albumin in rat liver. Biochem J. 1961 Mar;78:551–556. doi: 10.1042/bj0780551. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Geller D. M., Judah J. D., Nicholls M. R. Intracellular distribution of serum albumin and its possible precursors in rat liver. Biochem J. 1972 May;127(5):865–874. doi: 10.1042/bj1270865. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Grant P. T., Coombs T. L. Proinsulin, a biosynthetic precursor of insulin. Essays Biochem. 1970;6:69–92. [PubMed] [Google Scholar]
  6. Judah J. D., Nicholls M. R. Biosynthesis of rat serum albumin. Biochem J. 1971 Jul;123(4):649–655. doi: 10.1042/bj1230649. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Judah J. D., Nicholls M. R. The separation of intracellular serum albumin from rat liver. Biochem J. 1971 Jul;123(4):643–648. doi: 10.1042/bj1230643. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  9. Lazarow P. B., De Duve C. Intermediates in the biosynthesis of peroxisomal catalase in rat liver. Biochem Biophys Res Commun. 1971 Dec 3;45(5):1198–1204. doi: 10.1016/0006-291x(71)90145-8. [DOI] [PubMed] [Google Scholar]
  10. Milstein C., Brownlee G. G., Harrison T. M., Mathews M. B. A possible precursor of immunoglobulin light chains. Nat New Biol. 1972 Sep 27;239(91):117–120. doi: 10.1038/newbio239117a0. [DOI] [PubMed] [Google Scholar]
  11. SCHWERT G. W., TAKENAKA Y. A spectrophotometric determination of trypsin and chymotrypsin. Biochim Biophys Acta. 1955 Apr;16(4):570–575. doi: 10.1016/0006-3002(55)90280-8. [DOI] [PubMed] [Google Scholar]
  12. Schimke R. T., Doyle D. Control of enzyme levels in animal tissues. Annu Rev Biochem. 1970;39:929–976. doi: 10.1146/annurev.bi.39.070170.004433. [DOI] [PubMed] [Google Scholar]
  13. Schreiber G., Rotermund H. M., Maeno H., Weigand K., Lesch R. The proption of the incorporation of leucine into albumin to that into totaprotein in rat liver and hepatoma Morris 5123 TC. Eur J Biochem. 1969 Sep;10(2):355–361. doi: 10.1111/j.1432-1033.1969.tb00698.x. [DOI] [PubMed] [Google Scholar]
  14. Steiner D. F., Cunningham D., Spigelman L., Aten B. Insulin biosynthesis: evidence for a precursor. Science. 1967 Aug 11;157(3789):697–700. doi: 10.1126/science.157.3789.697. [DOI] [PubMed] [Google Scholar]
  15. Vaes G. The release of collagenase as an inactive proenzyme by bone explants in culture. Biochem J. 1972 Jan;126(2):275–289. doi: 10.1042/bj1260275. [DOI] [PMC free article] [PubMed] [Google Scholar]

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