Abstract
Human serum albumin (HSA) is the largest single protein component of plasma1 where its role is to maintain normal osmolarity and to act as a carrier for numerous small molecules (including nutrients and metabolites) many of which would otherwise have low solubility or be poorly tolerated in free solution. Compounds which it is capable of binding include fatty acids, bilirubin and numerous drugs.2 Unlike many recombinant proteins currently being considered by the biotechnology industry, albumin is already sold and used in large quantities.3 It is prepared by fractionation of donated blood and is used in the treatment of patients requiring fluid replacement.4 It is used particularly in the treatment of burn victims, those suffering from traumatic shock and some special groups of surgical patients. However its use is much affected by the custom and practice of particular countries and the preference of individual doctors.
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References
Peters, T. Jr, Serum Albumin. Adv. Prot. Chem., 37 (1985) 161–245.
Kragh-Hansen, U., Molecular aspects of ligand binding to serum albumin. Pharmacol Rev., 33 (1981) 17–57.
Klausner, A., Adjustment in the blood fraction market. Bio/Technology, 3 (1985) 119–25.
Jeans, E. R. A., Marshall, P. J. & Lowe, C. R., Plasma protein fractionation. Trends Biotechnol., 3 (1985) 267–70.
Meloun, B., Moravek, L. & Kostka, V., Complete amino acid sequence of human serum albumin. FEBS Lett., 58 (1975) 134–7.
Glaumann, H., Albumin secretory pathway in the hepatocyte. In Albumin Structure, Biosynthesis and Function, ed. T. Peters & I. Sjoholm. Pergamon Press, Oxford, 1978, pp. 41–50.
Andersson, L. O., Reduction and re-oxidation of the disulfide bonds of bovine serum albumin. Arch. Biochem. Biophys., 133 (1969) 277–85.
Kenten, J., Helm, B., Ishizaka, T., Cattini, P. & Gould, H., Properties of a human immunoglobulin epsilon-chain fragment synthesized in Escherichia coli. Proc. Natl. Acad. Sci. USA, 81 (1984) 2955–9.
Emtage, J. S., Angal, S., Doel, M. T., Harris, T. J. R, Jenkins, B., Lilley, G. & Lowe, P. A., Synthesis of calf prochymosin (prorennin) in Escherichia coli. Proc. Nat. Acad. Sci., USA, 80 (1983) 3671–5.
Simons, G., Remaut, E., Allet, B., Devos, R & Fiers, W., High-level expression of human interferon gamma in Escherichia coli under control of the pL promoter of bacteriophage lambda. Gene, 28 (1984) 55–64.
Latta, M., Knapp, M., Sarmientos, P., Brefort, G., Becquart, J., Guerrier, L., Jung, G. & Mayaux, J. F., Synthesis and purification of mature human serum albumin from Escherichia Coli. Bio/Technology, 5 (1987) 1309–14.
Hinchliffe, E., Kenny, E. & Leaker, A. J., Novel products from surplus yeast via recombinant DNA technology. In European Brewery Convention Symposium on Brewers Yeast Monograph XII. Verlag Hans Carl (Brauwelt-Verlag), Nurnberg, 1987, pp. 139–54.
Burton, S. J., Quirk, A. V & Wood, P. C, Refolding human serum albumin at relatively high protein concentration. Eur. J. Biochem., 179 (1989) 379–87.
Gray, G. L., Baldridge, J. S., McKeown, K. S., Heyneker, H. L. & Chang, C. N., Periplasmic production of correctly processed human growth hormone in Escherichia coli: natural and bacterial signal sequences are interchangeable. Gene, 39 (1985) 247–54.
Becker, G. W. & Hoiung, H. M., Expression, secretion and folding of human growth hormone in Escherichia coli. Purification and characterization. FEBS Lett., 204 (1986) 145–50.
Murray, R. G. E., Steed, P. & Elson, H. E., The location of the mucopeptide in sections of the cell wall of Escherichia coli and other Gram -ve bacteria. Can. J. Microbiol., 11 (1965) 547–60.
Novotny, A., Molecular aspects of endotoxic reactions. Bacteriol. Rev., 33 (1969) 72-98.
Saunders, C. W., Schmidt, B. J., Mallonee, K. L. & Guyer, M. S., Secretion of human serum albumin from Bacillus subtilis. J. Bacteriol., 169 (1987) 2917–25.
Schekman, R. & Novick, P., The secretory process and yeast cell-surface assembly. In The Molecular Biology of the Yeast Saccharomyces: Metabolism & Gene Expression, ed. J. N. Strathern, E. W. Jones & J. R. B. Broach. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, 1982, pp. 361–98.
Burrows, S., Baker’s yeast. In The Yeasts Vol. 3, ed. A. H. Rose & J. S. Harrison. Academic Press, New York, 1970, pp. 349–420.
Fiechter, A, Fuhrmann, G. F. & Kappeli, O., Regulation of glucose metabolism in growing yeast cells. Adv. Microb. Physiol., 22 (1981) 123–83.
Kingsman, S., Wilson, M. J., Cousens, D. J. & Hinchliffe, E., Yeast promoter. British Patent Application GB 8720396, 1986.
Condra, J. H., Ellis, R. W., Jones, R. E. & Schultz, L. D., Expression of recombinant proteins in yeast. European Patent Application EP0234862, 1987.
De Deken, R. H., The Crabtree effect: a regulatory system in yeast. J. Gen. Microbiol, 44 (1966) 149–56.
Sonnlietner, B. & Kaeppeli, O., Growth of Saccharomyces cerevisiae is controlled by its limited respiratory capacity: formulation and verification of a hypothesis. Biotechnol. Bioeng., 28 (1986) 9273–37.
Crabtree, H. G., Observations on the carbohydrate metabolism of tumors. Biochem. J., 23 (1929) 536–45.
von Meyenburg, K. H., Energetics of the budding cycle of Saccharomyces cerevisiae during glucose limited aerobic growth. Arch. Microbiol., 66 (1969) 289–303.
Fiechter, A. & von Meyenburg, K. H., Automatic analysis of gas exchange in microbial systems. Biotech. Bioengng 10 (1968) 535–49.
Lloyd, D., Kristensen, B. & Degn, H., Glycolyis and respiration in yeasts: the effect of ammonium ions studied by mass spectrometry. J. Gen. Microbiol., 129 (1983) 2125–7.
Wang, H. Y, Cooney, C. L. & Wang, D. I. C, Computer control of bakers’ yeast production. Biotechnol. Bioengng, 21 (1979) 975–95.
Walter, P., Signal recognition. Two receptors act sequentially. Nature, 328 (1987) 763–4.
Verner, K. & Schatz, G., Protein translocation across membranes. Science, 241 (1988) 1307–13.
Walter, P. & Lingpappa, V., Mechanism of protein translocation across the endoplasmic reticulum membrane. Ann. Rev. Cell Biol., 2 (1986) 499–516.
Rapoport, T. A., Protein translocation across and integration into membranes. CRC Crit. Rev. Biochem., 20 (1986) 73–137.
Blobel, G. & Dobberstein, B., Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J. Cell Biol., 67 (1975) 835–51.
Walter, P., Ibrahimi, I. & Blobel, G., Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein. J. Cell Biol., 91 (1981) 545–50.
Gilmore, R., Blobel, G. & Walter, P., Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle. J. Cell Biol., 95 (1982) 463–9.
Schatz, G., Protein translocation: a common mechanism for different membrane systems. Nature, 321 (1986) 108–9.
Baker, R. K., Bentivoglio, G. P. & Lively, M. O., Partial purification of microsomal signal peptidase from hen oviduct. J. Cell Biochem., 32 (1986) 193–200.
Bohni, P. C., Deshaies, R. J. & Schekman, R. W., SEC11 is required for signal peptide processing and yeast cell growth. J. Cell Biol., 106 (1988) 1035–42.
Peters, T. & Davidson, L. K., The biosynthesis of rat serum albumin. In vivo studies on the formation of the disulfide bonds. J. Biol Chem., 257 (1982) 8847–53.
Lang, K. & Schmid, F. X., Protein-disulphide isomerase and prolyl isomerase act differently and independently as catalysts of protein folding. Nature, 331 (1988) 453–5.
Fuchs, S., De Lorenzo, F. & Anfinsen, C. B., Studies on the mechanism of the enzymic catalysis of disulfide interchange in proteins. J. Biol. Chem., 242 (1967) 398–402.
Fischer, G., Bang, H. & Mech, C, Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in proline-containing peptides. Biochim. Biophys. Acta, 43 (1984) 1101–11.
Julius, D., Schekman, R. & Thorner, J., Glycosylation and processing of prepro-alpha-factor through the yeast secretory pathway. Cell, 36 (1984) 309–18.
Rothman, J. E. & Lodish, H. F., Synchronised transmembrane insertion of glycosylation of a nascent membrane protein. Nature, 269 (1977) 775–80.
Berger, M. & Schmidt, F., Protein fatty acyltransferase is located in the rough endoplasmic reticulum. FEBS Lett., 187 (1985) 289–94.
Pfeffer, S. R. & Rothman, J. E., Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi. Ann. Rev. Biochem., 56 (1987) 829–52.
Rose, J. K. & Doms, R. W., Regulation of protein export from the endoplasmic reticulum. Ann. Rev. Cell Biol., 4 (1988) 257–88.
Schekman, R., Protein localization and membrane traffic in yeast. Ann. Rev. Cell Biol., 1 (1985) 115–43.
Das, R. C. & Shultz, J. L., Secretion of heterologous proteins from Saccharomyces cerevisiae. Biotechnol. Progress, 3 (1987) 43–8.
Kurjan, J. & Herskowitz, I., Structure of a yeast pheromone (MF alpha): a putative alpha-factor precursor contains four tandem copies of mature alpha-factor. Cell., 30 (1982) 933–43.
Julius, D., Brake, A., Blair, L., Kunisawa, R. & Thorner, J., Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-alpha-factor. Cell, 37 (1984) 1075–89.
Julius, D., Blair, L., Brake, A., Sprague, G. & Thorner, J., Yeast alpha factor is processed from a larger precursor polypeptide: the essential role of a membrane-bound dipeptidyl aminopeptidase. Cell., 32 (1983) 839–52.
Achstetter, T. & Wolf, D. H., Hormone processing and membrane-bound proteinases in yeast. EMBO J., 4 (1985) 173–7.
Bitter, G. A, Chen, K. K., Banks, A. R. & Lai, P.-H., Secretion of foreign proteins from Saccharomyces cerevisiae directed by alpha-factor gene fusions. Proc. Nat. Acad. Sci., USA, 81 (1984) 5330–4.
Zsebo, K. M., Lu, H.-S., Fieschko, J. C, Goldstein, L., Davis, J., Duker, K., Suggs, S. V., Lai, P.-H. & Bitter, G. A., Protein secretion from Saccharomyces cerevisiae directed by alpha-factor leader region. J. Biol Chem., 261 (1986) 5858–65.
Carter, B. L. A, Doel, S., Goodey, A. R., Piggot, J. R. & Watson, M. E. W., Secretion of mammalian polypeptides by yeast. Microbiol. Sci., 3 (1986) 23–7.
Sleep, D., Belfield, G. P. & Goodey, A. R., The secretion of human serum albumin by Saccharomyces cerevisiae. Yeast, 4 (1988 Spec. Iss.) S168.
Dugaiczyk, A, Law, S. W. & Dennison, O. E., Nucleotide sequence and the encoded amino acids of human serum albumin mRNA. Proc. Nat. Acad. Sci., USA, 79 (1982) 71–5.
Brennan, S. O., Owen, M. C, Boswell, D. R., Lewis, J. H. & Carrell, R. W., Circulating proalbumin associated with a variant proteinase inhibitor. Biochim. Biophys. Acta, 802 (1984) 24–8.
Brennan, S. O. & Carrell, R. W., A circulating variant of human proalbumin. Nature, 274 (1978) 908–9.
Bathurst, I. C., Brennan, S. O., Carrell, R. W., Cousens, L. S., Brake, A. I. & Barr, P. J., Yeast KEX2 protease has the properties of a human proalbumin converting enzyme. Science, 235 (1987) 348–50.
Sleep, D., Belfield, G. P. & Goodey, A. R., The secretion of human serum albumin by the yeast Saccharomyces cerevisiae. Bio/Technology, (submitted).
Futcher, A. B. & Cox, B. S., Maintenance of the 2-micron circle plasmid in populations of Saccharomyces cerevisiae. J. Bacteriol., 154 (1984) 612–22.
Broach, J. R., Construction of high copy yeast vectors fusing 2-micron circle sequences. Methods Enzymol., 101 (1983) 307–25.
Tubb, R. S., 2-micron DNA plasmid in brewery yeasts. J. Inst. Brew., 86 (1980) 78–80.
Broach, J. R., The yeast plasmid 2-micron circle. In The Molecular Biology of the Yeast Saccharomyces Life Cycle & Inheritance, ed. J. N. Strathern, E. W. Jones & J. R. B. Broach. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, 1981, pp. 445–70.
Futcher, A. B. & Cox, B. S., Copy number and the stability of 2-micron circle-based artificial plasmids of Saccharomyces cerevisiae. J. Bacteriol., 157 (1984) 283–90.
Jayaram, M, Sutton, A., & Broach, J. R., Properties of REP3: a cis-acting locus required for stable propagation of the Saccharomyces cerevisiae plasmid 2-microns circle. Mol. Cell Biol., 5 (1985) 2466–75.
Kikuchi, Y., Yeast plasmid requires a cis-acting locus and two plasmid proteins for its stable maintenance. Cell, 35 (1983) 487–93.
Beggs, J. D., Multiple-copy yeast plasmid vectors. Alfred Benzon Symposium, 16 (1981) 383–95.
Murray, A. W. & Szostak, J. W., Pedigree analysis of plasmid segregation in yeast. Cell, 34 (1983) 961–70.
Cashmore, A. M., Albury, M. S., Hadfield, C. & Meacock, P. A, Genetic analysis of partitioning functions encoded by the 2 μm circle of Saccharomyces cerevisiae. Mol. Gen. Genet., 203 (1986) 154–62.
Jayarum, M., Li, Y. Y. & Broach, J. R., The yeast plasmid 2 μm circle encodes components required for its high copy propagation. Cell., 34 (1983) 95–104.
Futcher, A. B., The 2-micron circle plasmid of Saccharomyces cerevisiae. Yeast, 4 (1988) 27–40.
Chinery, S. A & Hinchliffe, E., The stable maintenance of 2-micron plasmids in yeast: a new class of vector. Yeast, 4 (1988 Spec. Iss.) S123.
Guerineau, M., Grandchamp, C. & Slonimski, P., Circular DNA of a yeast episome with two inverted repeats: structural analysis by a restriction enzyme and electron microscopy. Proc. Nat Acad. Sci., USA, 73 (1976) 3030–4.
Hartley, J. L. & Donelson, J. E., Nucleotide sequence of the yeast plasmid. Nature, 286 (1980) 860–5.
Blanc, H., Gerbaud, C., Slonimski, P. & Guerineau, M., Stable yeast transformation with chimeric plasmids using a 2-micron-circular DNA-less strain as a recipient. Mol. Gen. Genet., 176 (1979) 335–42.
Broach, J. R. & Hicks, J. B., Replication and recombination functions associated with the yeast plasmid, 2μ circle. Cell., 21 (1980) 501–8.
Gubbins, E. J., Newlon, C. S., Kann, M. D. & Donelson, J. E., Sequence organization and expression of a yeast plasmid DNA. Gene, 1 (1977) 185–207.
Fuchter, A. B., Copy number amplification of the 2-micron circle plasmid of Saccharomyces cerevisiae. J. Theor. Biol., 119 (1986) 197–204.
Volkert, F. C. & Broach, J. R., Site-specific recombination promotes plasmid amplification in yeast, Cell., 46 (1986) 541–50.
Murray, J. A, Scarpa, M., Rossi, N. & Cesareni, G., Antagonistic controls regulate copy number of the yeast 2 μ plasmid. EMBO J., 6 (1987) 4205–12.
Reynolds, A. E., Murray, A. W. & Szostak, J. W., Roles of the 2-micron gene products in stable maintenance of the 2-micron plasmid of Saccharomyces cerevisiae. Mol. Cell Biol., 7 (1987) 3566–73.
Som, T., Armstrong, K. A, Volkert, F. C. & Broach, J. R., Autoregulation of 2-micron circle gene expression provides a model for maintenance of stable plasmid copy levels. Cell., 52 (1988) 27–37.
McLeod, M., Craft, S. & Broach, J. R., Identification of the crossover site during FLP-mediated recombination in the Saccharomyces cerevisiae plasmid 2-microns circle. Mol. Cell Biol., 6 (1986) 3357–67.
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Collins, S.H. (1990). Production of Secreted Proteins in Yeast. In: Harris, T.J.R. (eds) Protein Production by Biotechnology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1565-0_5
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