Learn about notable biologics discoveries and best practices from our knowledgeable team

co-edited by dr. steveN chamow

Therapeutic Fc-Fusion Proteins

Edited by three pioneers in the field, each with longstanding experience in the biotech industry, and a skilled scientific writer, this is the first book to cover every step in the development and production of immunoglobulin Fc-fusion proteins as therapeutics for human disease: from choosing the right molecular design, to pre-clinical characterization of the purified product, through to batch optimization and quality control for large-scale cGMP production. 

Published in 2014.


Critical Praise for Therapeutic Fc-Fusion Proteins

“An informative, comprehensive review of the field and a valuable reference text.”

– Michael E. Ultee, Chief Scientific Officer, Gallus Biopharmaceuticals

“A strong theoretical background supported by the profound professional experience of the authors.”

 – Dr. Pedro Berraondo, Center for Applied Medical Research (CIMA), Pamplona, Spain

co-edited by dr. steveN chamow

Antibody Fusion Proteins

Recent developments in the field of protein engineering have seen an emergence of genetically engineered fusion molecules derived from antibodies—often used as important and beneficial molecular tools in research. Antibody Fusion Proteins provides essential information on several types of these antibody fusion proteins. The book examines the construction, properties, applications, and problems associated with specific types of fusion molecules used in clinical and research medicine.

Published in 1999.

Chamow and Associates Book Review

(2012) Pharmaceutical Biotechnology: Drug Discovery and Clinical Applications, 2nd Ed., O. Kayser and H. Warzecha, eds.) Wiley-VCH, 2012. Biotechnol. J. 7, 1061-1062.

Chamow, S.M., and Mize, N.

Chamow and Associates Review Articles

(2021) Buffers. Navigating New Demands on Downstream Raw Materials. BioProcess Intl. eBooks Mar issue

Shwa, R., Linderholm, A., Bratt, J., Chamow, S.M.

(2018) Therapeutic IgG-Like Bispecific Antibodies Modular Versatility and Manufacturing Challenges, Part 2. BioProcess Intl. Jan issue

Bratt, J., Linderholm, A., Monroe, B., Chamow, S.M.

(2017) Therapeutic IgG-Like Bispecific Antibodies Modular Versatility and Manufacturing Challenges, Part 1. BioProcess Intl. Dec issue

Bratt, J., Linderholm, A., Monroe, B., Chamow, S.M.

(2017) Buffers in Biologics Manufacturing. BioProcess Intl. Feb issue

Bratt, J., Chamow, S.M., Green, D.G., Linderholm, A.

(2014) Immunoglobulin Fc-Fusion Proteins Part 2: Therapeutic Uses and Clinical Development. BioProcess Intl. Nov issue

Linderholm, A., and Chamow, S.M.

(2014) Immunoglobulin Fc-Fusion Proteins Part 1: Their Design and Manufacture. BioProcess Intl. Oct issue

Linderholm, A., and Chamow, S.M.

Chamow and Associates Refereed Articles

(2021) Generation of recombinant hyperimmune globulins from diverse B-cell repertoires. Nature Biotechnology. April issue

Keating, Sheila M., Mizrahi, Rena A., Adams, Matthew S., et. al.

(2020) Capture of CH1-Containing Bispecific Antibodies: Evaluating an Alternative to Protein A. BioProcess Int'l. May issue

Chamow S.M., Pratap, P.P., Linderholm, A., Harris, K.E., Schellenberger, U., and Jorgensen, B.

(2011) NMR structure of human thymosin alpha-1. Biochem. Biophys. Res. Comm. 416, 356-361.

Elizondo-Riojas, M.A., Chamow, S.M., Tuthill, C.W., Gorenstein, D.G., and Volk, D.

Steven Chamow Review Articles

  • Chen, B., Zapata, G., and Chamow, S.M. (2004) Strategies for rapid development of liquid and lyophilized antibody formulations. BioProcess Intl. Jan issue, pp. 48-52.
  • Chadd, H.E., and Chamow, S.M. (2001) Therapeutic antibody expression technology. Curr. Opinion Biotechnol. 12, 188-194. Download PDF
  • Ashkenazi, A., and Chamow, S.M. (1997) Immunoadhesins as research tools and therapeutic agents. Curr. Opinion Immunol. 9, 195-200.
  • Chamow, S.M., and Ashkenazi, A. (1996) Immunoadhesins: Principles and applications. Trends in Biotechnology 14, 52-60. Download PDF
  • Chamow, S.M., Zhang, D.Z., Mhatre, S.M., Tan, X.Y., Peers, D.H., Marsters, S.A., Byrn, R.A., Ashkenazi, A., and Junghans, R.P. (1995) A humanized, bispecific immunoadhesin-antibody that retargets CD3+ effectors to kill HIV-1 infected cells. J. Hematother. 4, 439-446.
  • Ashkenazi, A., and Chamow, S.M. (1995) Immunoadhesins: an alternative to human monoclonal antibodies. Methods: A Companion to Methods in Enzymology 8, 104-115.Chamow, S.M., Duliege, A.M., Ammann, A., Kahn, J.O., Allen, J.D., Eichberg, J.W., Byrn, R.A., Capon, D.J., Ward, R.H.R., and Ashkenazi, A. (1992) CD4 immunoadhesins in anti-HIV therapy: New developments. Intl. J. Cancer 52, Supplement 7, 69-72.
  • Dean, J., Chambelain, M.E., Millar, S.E., Ringuette, M.J., Philpott, C.C., Baur, A.W., and Chamow, S.M. (1989) Developmental expression of ZP3, a mouse zona pellucida gene. In Development of Preimplantation Embryos and Their Environment. (K. Yoshinaga and T. Mori, eds.), pp. 21-32, Alan R. Liss, NY.
  • Chambelain, M.E., Ringuette, M., Philpott, C.C., Chamow, S.M., and Dean, J. (1989) Molecular genetics of the mouse zona pellucida. In The Mammilian Egg Coat: Structure and Function, (J. Deitl, ed.), pp. 1-17, Springer-Verlag, Berlin.
  • Dean, J., Ringuette, M., Sobieski, D.A., East, J.J., and Chamow, S.M. (1986) Molecular genetics of the mouse zona pellucida: Implications for fertilization and early development. In Immunological Approaches to Contraception and Promotion of Fertility (G.P. Talwar, ed.), pp. 241-249, Plenum Press, NY.

Steven Chamow Refereed Articles

  • Keck, R., Nayak, K., Lerner, L., Raju, S., Ma, S., Schreitmuller, T., Chamow, S., Moorhouse, K., Kotts, C. and Jones, A. (2008) Characterization of a complex glycoprotein whose variable metabolic clearance in humans is dependent on terminal N-acetylglucosamine content. Biologicals 36(1), 49-60.
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  • Chen, B., Bautista, R., Yu, K., Mulkerrin, M., Zapata, G. and Chamow, S.M. (2003) Influence of histidine on the stability and physical properties of a fully human antibody in aqueous and solid forms. Pharmaceutical Research 12, 1952-60.
  • Chun, C., Heineken, K., Szeto, D., Ryll, T. Chamow, S.M., and Chung, J.D. Application of factorial design to accelerate identification of CHO growth factor requirements. (2003) Biotechnol. Prog. 19, 52-57.
  • Raju, T.S., Briggs, J.B., Chamow, S.M., Winkler, M.E., and Jones, A.J.S. (2001) Glycoengineering of therapeutic glycoproteins: in vitro galactosylation and sialylation of glycoproteins with terminal N-acetylglucosamine and galactose residues. Biochemistry 40, 8868-8876. Download PDF
  • Weikert, S., Papac, D., Briggs, J., Cowfer, D., Tom, S., Gawlitzek, M., Lofgren, J., Mehta, S., Chisholm, V., Modi, N., Eppler, S., Carroll, K., Chamow, S.M., Peers, D., Berman, P, and Krumman, L. (1999) Engineering Chinese hamster ovary cells to maximize sialic acid content of recombinant glycoproteins. Nat.Biotechnol.17(11), 1116-1121. Download PDF
  • Kohne, C., Johnson, A., Tom, S., Peers, D.H., Gehant, R.L., Hotaling, T.A., Brousseau, D., Ryll, T., Fox, J.A., Chamow, S.M., and Berman, P.W. (1999) Secretion of glycosylation site mutants can be rescued by the signal/pro sequence of tissue plasminogen activator. J. Cell Biochem., 75(3), 446-461. Download PDF
  • Pender, S.L., Fell, J.M., Chamow, S.M., Ashkenazi, A., and MacDonnald, T.T. (1998) A p55 TNF receptor immunoadhesin prevents T-cell mediated intestinal injury by inhibiting matrix metalloproteinase production. J. Immunol.160(8), 4098-4103. Download PDF
  • Logan, K.L., Lagerlund, I., and Chamow, S.M. (1998) A simple, two-component buffer enhances use of chromatofocusing for processing of therapeutic proteins. Biotech. Bioeng. 62, 208-215. Download PDF
  • Van Zee, K.J., Moldawer, L.L., Oldenburg, H.S.A., W.A., T., Stackpole, S.A., Montegut, W.J., Rogy, M.A., Meschter, C., Gallati, H., Schiller, C-D., Richter, W.F., Loetscher, H., Ashkenazi, A., Chamow, S.M., Wurm, F., Calvano, S.E., Lowry, S.F., and Lesslauer, W. (1996) Protection against lethal E. coli bacteremia in baboons (Papio annubis) by pretreatment with a 55 kDa TNF receptor (CD120a)-Ig fusion protein, Ro 45-2081. J. Immunol. 156, 2221-2230.
  • Zioncheck, T.F., Richardson, L., Liu, J., Chang, L., King, K., Bennet, G.L., Fugedi, P., Chamow, S.M., Schwall, R.H., and Stack, R.J. (1995) Sulfated oligosaccharides promote hepatocyte growth factor association and govern its mitogenic activity. J. Biol. Chem. 270, 16871-16878.
  • Roos, F., Ryan, A.M., Chamow, S.M., Bennet, G.L., and Schwall, R.H. (1995) Induction of liver growth in normal mice by infusion of hepatocyte growth factor/scatter factor. Am. J. Physiol. 268, (Gastrointest. Liver Physiol. 31) G380-G386.
  • Chamow, S.M., Zhang, D.Z., Mhatre, S.M., Tan, X.Y., Peers, D.H., Marsters, S.A., Byrn, R.A., Ashkenazi, A., and Junghans, R.P. (1994) A humanized bispecific immunoadhesin-antibody that retargets CD3+ effectors to kill HIV-1 infected cells. J. Immunol. 153, 4268-4280.
  • Pitti, R.M., Marsters, S.A., Haak-Frendscho, M., Osaka, G., Mordenti, J., Chamow, S.M., and Ashkenazi, A. (1994) Molecular and biological properties of an IL-1 receptor immunoadhesin. Molec. Immunol. 31, 1345-1351.
  • Beck, J., Marsters, S.A., Harris, R.H., Carter, P., Ashkenazi, A., and Chamow, S.M. (1994) Generation of soluble IL-1 receptor from an immunoadhesin by specific cleavage. Molec. Immunol. 31, 1335-1344.
  • Jin, H., Yang, R., Marsters, S.A., Bunting, S.A., Wurm, F.M., Chamow, S.M., and Ashkenazi, A. (1994) Protection against rat endotoxic shock by p55 TNF receptor immunoadhesin: Comparison with anti-TNF monoclonal antibody. J. Infect. Dis. 170, 1323-1326.
  • Flasher, D., Konopka, K., Chamow, S.M., Dazin, P., Ashkenazi, A., Pretzer, E., and Duzgunes, N. (1994) Liposome targeting to HIV-1 infected cells via sCD4 and CD4-IgG. Biochem. Biophys. Acta. 1194, 185-196.
  • Chamow, S.M., Kogan, T.P., Venuti, M., Gadek, T., Peers, D.H., Harris, R.J., Mordenti, J., Shak, S., and Ashkenazi, A. (1994) Modification of CD4 immunoadhesin with monomethoxypolyethylene glycol aldehyde via reductive alkylation. Bioconjugate Chem. 5. 133-140. Download PDF
  • Haak-Frendscho, M., Marsters, S.A., Chamow, S.M., Peers, D.H., Simpson, N.J., and Ashkenazi, A. (1993) Inhibition of interferon-γγby an interferon-γ receptor immunoadhesin. Immunology 79, 594-599.
  • Roos, F., Terrell, T.G., Godowski, P.J., Chamow, S.M., and Schwall, R.H. (1992) Reduction of ααnaphthylisothiocyanate-induced hepatoxicity by recombinant human hepatocyte growth factor. Endocrinology 131, 2540-2544.
  • Chamow, S.M., Kogan, T.P., Peers, D.H., Hastings, R.C., Byrn, R.A., and Ashkenazi, A. (1992) Conjugation of soluble CD4 without loss of biological activity via a novel carbohydrate-directed crosslinking reagent. J. Biol. Chem. 267, 15916-15922. Download PDF
  • Ashkenazi, A., Marsters, S.A., Capon, D.J., Chamow, S.M., Figari, I.S., Pennica, D., Goeddel, D.V., Palladino, M.A., and Smith, D.H. (1991) Protection against endotoxic shock by a soluble tumor necrosis factor receptor immunoadhesin. Proc. Natl. Acad. Sci. USA 88, 10535-10539.
  • Chamow, S.M., Peers, D.H., Byrn, R.A., Mulkerrin, M.G., Harris, R.J., Wang, W.C., Bjorkman, P.J., Capon, D.J., and Ashkenazi, A. (1990) Enzymatic cleavage of a CD4 immunoadhesin generates crystallizable, biologically active Fd-like fragments. Biochemistry 29, 9885-9891. Download PDF 
  • Sekigawa, I., Chamow, S.M., Groopman, J.E., and Byrn, R.A. (1990) CD4 immunoadhesin, but not recombinant soluble CD4, blocks syncytium formation by human immunodeficiency of CD4 immunoadhesin. J. Virol. 64, 5194-5198.
  • Byrn, R.A., Mordenti, J., Lucas, C., Smith, D., Marsters, S.A., Johnson, J.S., Chamow, S.M., Wurm, F.M., Gregory, T., Groopman, J.E., and Capon, D.J. (1990) Biological properties of a CD4 immunoadhesin. Nature 344, 667-670.
  • Harris, R.J., Chamow, S.M., Gregory, T.J., and Spellman, M.W. (1990) Characterization of a soluble form of human CD4: Peptide analyses confirm the expected amino acid sequence, identify glycosylation sites and demonstrate the presence of three disulfide bonds. Eur. J. Biochem. 188, 291-300.
  • Liang, L.F., Chamow, S.M., and Dean, J. (1990) Oocyte-specific expression of ZP2: Developmental regulation of the zona pellucida genes. Molec. and Cell. Biol. 10, 1507-1515
  • Capon, D.J., Chamow, S.M., Modenti, J., Marsters, S.A., Gregory, T., Mitsuya, H., Byrn, R.A., Lucas, C., Wurm, F.M., Groopman, J.E., Broder, S., and Smith, D.H., (1989) Designing CD4 immunoadhesins for AIDS therapy. Nature 337, 525-531. Download PDF
  • Byrn, R.A., Sekigawa, I., Chamow, S.M., Gregory, T.J., Capon, D.J., and Groopman, J.E. (1989) Characterization of in vitro inhibition of HIV by purified recombinant CD4. J. Virol. 63, 4370-4375. Download PDF 
  • Millar, S.E., Chamow, S.M., Baur, A.W., Oliver, C., Robey, F., and Dean, J. (1989) A contraceptive vaccine: Isoimmunization with a zona pellucida peptide deduced from cloned mouse ZP3 cDNA. Science 246, 935-938.
  • Chamow, S.M., and Hedrick, J.L. (1988) A micromethod for the estimation of oligosaccharides containing glycosidically linked sialic acid or hexoses, or both, in glycoproteins. Carbohydrate Res. 176, 195-203.
  • Ringuette, M., Sobieski, D., Chamow, S.M., and Dean, J. (1986) Ooctye-specific gene expression: Molecular characterization of a cDNA coding for ZP3, the sperm receptor of the mouse zona pellucida. Proc. Natl. Acad. Sci. USA 83, 4341-4345.
  • Chamow, S.M., and Hedrick, J.L. (1986) Subunit structure of a cortical granule lectin involved in the block to polyspermy in Xenopus laevis eggs. FEBS Letters 206, 353-357.