Recombinant bovine somatotropin

Capper, J. L., Castaneda-Gutierrez, E., Cady, R. A., and Bauman, D. E. (2008). The environmental impact of recombinant bovine somatotropin (rbST) use in dairy production. Proc. Natl. Acad. Sci. USA 105, 9668-9673. 

Hagemann et al. [3.13] calculated the absorption isotherms for recombinant bovine Somatotropin (rbSt) and found 5-8 g water in 100 g protein, which was not only on the surface but also inside the protein molecule. 

Recognition site mapping, 10 326 Recombinant bovine somatotropin, 13 2 Recombinant CHO cell products... 

There are many examples of ELIS As used for detecting host cell impurities in the literature. Pauly et al.12 developed an ELISA to detect impurities in erythropoietin that had a detection limit of around 0.05 ng/ml. SDS polyacrylamide gel and Western blot analysis were used to confirm the spectrum of proteins detected and to demonstrate the specificity of the antibody preparation. Anicetti et al.14 describe an assay for the detection of E. coli proteins in recombinant DNA-derived human growth hormone. Whitmire and Eaton15 report on an immuno-ligand assay for quantitation of process-specific E. coli host cell contaminant proteins in a recombinant bovine somatotropin. 

Whitmire, M.L. and L.C. Eaton (1997). An immunoligand assay for quantitation of process specific Escherichia coli host cell contaminant proteins in a recombinant bovine somatotropin. J Immunoassay 18(1) 49-65. 

This polypeptide hormone constitutes one form of the recombinant bovine somatotropins used to increase milk production in dairy cows. Several studies have been performed in the United States, United Kingdom, and Germany to determine the concentrations of this drug in milk (99, 100). 

Hageman et al. [3.13] calculated the absorption isotherms for recombinant bovine somatotropin (rbSt) and found 5-8 g of water in 100 g of protein, which was not only on the surface but also inside the protein molecule. Costantino et al. [3.72] estimated the water monolayer M0 (g/100 g dry protein) for various pharmaceutical proteins and for their combination with 50 wt% trehalose or mannitol as excipient. They compared three methods of calculating MQ (1) theoretical (th) from the strongly water binding residues, (2) from conventional adsorption isotherm measurements (ai) and (3) from gravimetric sorption analysis (gsa) performed with a microbalance in a humidity-controlled atmosphere. Table 3.5 summarizes the results for three proteins. The methods described can be helpful for evaluating RM data in protein formulations. 

Azzara, C.D., Dimick, P.S., Chalupa, W. 1987. Milk lipoprotein lipase activity during long-term administration of recombinant bovine somatotropin. J. Dairy Sci. 70, 1937-1940. 

Recombinant bovine somatotropin, lysozyme Both the excipient type (sucrose, sorbitol, glycerol) and moisture content affected protein degradation [30]... 

C.L. Stevenson, M.J. Hageman, Estimation of recombinant bovine somatotropin solubility by excluded-volume interaction with polyethylene glycols, J. Pharm. Sci. 12 (1995) 1671—1676. 

K Tsuji. Evaluation of sodium dodecyl sulfate non-acrylamide polymer gel-filled capillary electrophoresis for molecular size separation of recombinant bovine somatotropin. J Chromatogr 652 139-147, 1993. 

Company s recombinant bovine somatotropin (BST) into the veterinary food animal market. BST, also known as bovine growth hormone, rbST, rbGH, sometribove, and Posilac , is a drug designed to increase milk production in dairy cows. 

Cmzan, S.M. HHS News Release, P93-40, Recombinant Bovine Somatotropin, U.S. Department of Health and Human Services, Washington, D.C., November 5, 1993. 

Chang, J.R Tucker, R.C. Christ, B.F. Coleman, M.R. Non-denaturing assay for the determination of the potency of recombinant bovine somatotropin by high-performance size-exclusion chromatography. J.Chromatogr.A, 1994, 675, 113—122... 

This part will mainly focus on host cell proteins (HCPs) quantification. Process-specific HCP assays are in general targeted to be in place prior to the initiation of phase III clinical trials. Immunoassays are the most specific and sensitive techniques available for detecting and quantifying protein impurities. There are two methods commonly employed to quantify protein impurities in biopharmaceuticals enzyme-linked immunosorbent assays (ELISA) and immunoligand assays (ILA). Both methods are able to detect very low ppm level of impurities. ELISA have been developed to measure host protein impurities in a number of recombinant proteins including human growth hormone (Anicetti et ah, 1986), insulin (Baker et al, 1981) and staphylokinase (Wan et ah, 2002). ILA assays have been used to detect protein impurities in recombinant bovine somatotropin (Whitmire and Eaton,... 

Moseley, M., Paulissen, J. B., Goodwin, M. C., Alaniz, G. R., and Claflin, W.H., 1992, Recombinant bovine somatotropin improves growth performance in finidiing beef steers, J. Anim. Sci. 70 412-425. 

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