but not by glycosylation inhibitor,
tunicamycin, in human prostate cancer cells. J. Cell
Biochem., 77, 396-408 (2000).
10. Aagaard-Tillery, K.M., and Jelinek, D.F., Differential
activation of a calcium-dependent
but not by glycosylation inhibitor,
tunicamycin, in human prostate cancer cells. J. Cell
Biochem., 77, 396-408 (2000).
8. Aagaard-Tillery, K.M., and Jelinek, D.F., Differential
activation of a calcium-dependent
Targets and Biomarker Discovery (M. Sioud, ed.).
Humana Press (Totowa, NJ), Vol. 360, pp. 57-89
(2007).
4. Subramanyam, S., and Spies, M., Methods
Enzymol., 600, 157-178 (2018).
5. Okkelman, I.A
Acad. Sci. USA, 77, 4666 (1980).
3. Chaiet, L. and Wolf, F.J., Arch. Biochem. Biophys.,
106, 1 (1964).
4. Bayer, E.A., Ben-Hur, H. and Wilchek, M., in Meth.
Enzymol., 184, 80-89 (1990).
5. Techniques
(1963) Biochem. Biophys. Acta
77:383.
2. Mossman, T. (1983) J. Immunol. Methods
65:55.
3. Denizot, F. and Lang, R. (1986) J. Immunol.
Methods 89:271.
4. Carmichael, J. et al. (1987) Cancer
al. Biochemistry, 27,
797 (1988).
14. Todaro, G. J., et al., Proc. Natl. Acad. Sci. USA,
77, 5258 (1980).
15. Blomquist, M. C., et al., Proc. Natl. Acad. Sci.
USA, 81, 7363
Salmonella Paratyphi.
4. Public Health Laboratory Service, Monograph Series No. 8, Public Health Laboratory Service,
London,
England (1974)
5. R.W.S. Harvey, T.S. Price, J. Hyg. Camb., 77, 333 (1976)
RP-HPLC chromatogram
resolving the α- and β-
subunits of CellPrime® rTrypsin.
Peak area indicates 77 %
β-trypsin and 14 % α-trypsin.
The profile highlights the high
degree of CellPrime® rTrypsin
purity