Abstract
Lysozyme from hen egg white was identified as an immunoglobulin production stimulating factor (IPSF) which enhances immunoglobulin production by hybridomas and lymphocytes. The IPSF activity of lysozyme was facilitated by heat treatment. The heat treatment of lysozyme at 83°C for 30 min activated its stimulating effect 15.9-fold compared with that of native lysozyme. The IPSF activity of lysozyme heat-treated in 4 M urea solution was enhanced 8.8-fold than that of native lysozyme. However, the IPSF activity of lysozyme in 4 M urea solution without heat treatment was completely lost. The uptake of lysozyme by hybridoma cells was enhanced by heat denaturation in 4 M urea. This indicates that heat-treated lysozyme in 4 M urea is easily taken by HB4C5 cells and expresses high IPSF activity in the cells. Moreover, coexistence of 2-mercaptoethanol during heat denaturation in 4 M urea solution extremely enhanced the IPSF activity of lysozyme up to 77.8-fold.
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References
Murakami, F., Sasaki, T., and Sugahara, T.: Lysozyme stimulates immunoglobulin production by human-human hybridoma and human peripheral blood lymphocytes, Cytotechnology 24 (1997). 177–182.
Sugahara, T., Murakami, F., Yamada, Y., and Sasaki, T.: The mode of actions of lysozyme as an immunoglobulin production stimulating factor, Btochtm. Btophys. Acta 1475 (2000), 27–34.
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© 2002 Springer Science+Business Media Dordrecht
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Sugahara, T., Yamada, Y., Ueda, Y., Matsubara, S., Sasaki, T. (2002). Immunoglobulin Production Stimulating Activity of Heat-Denatured Lysozyme. In: Shirahata, S., Teruya, K., Katakura, Y. (eds) Animal Cell Technology: Basic & Applied Aspects. Animal Cell Technology: Basic & Applied Aspects, vol 12. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-0728-2_32
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DOI: https://doi.org/10.1007/978-94-017-0728-2_32
Publisher Name: Springer, Dordrecht
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