Enhancement of Immunoglobulin Productivity of Human–Human Hybridoma HB4C5 Cells by Basic Proteins and Poly-basic Amino Acids
Author(s) -
Takuya Sugahara,
Takeshi Sasaki,
Hiroki Murakami
Publication year - 1994
Publication title -
bioscience, biotechnology, and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.58.2212
Subject(s) - productivity , library science , computer science , economics , macroeconomics
Immunoglobulin M productivity of a human-human hybridoma line, HB4C5, was enhanced by the addition of histones H1, H2A, and H2B in serum-free medium, which are lysine-rich histones. On the contrary arginine-rich histones, histone H3 and H4, did not stimulate immunoglobulin production at all. Another arginine-rich protein, protamine also did not significantly stimulate immunoglobulin production. These results suggested that there is a correlation between amino acid residues of basic proteins and stimulation of immunoglobulin production. In this connection, immunoglobulin production stimulating activities of poly-lysine and poly-arginine were investigated. Both poly-L-lysine and poly-D-lysine stimulated IgM productivity of the human-human hybridomas. These results show that the enhancing effect of lysine residues was derived from its physiochemical features. On the other hand, poly-L-arginine did not enhance the productivity.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom