TY - JOUR
T1 - Antigen-specific augmentation factor involved in murine delayed-type footpad reaction. I. Nature of augmentation factor
AU - Nakamura, Seiji
AU - Himeno, Kunisuke
AU - Yamada, Akira
AU - Kawamura, Ikuo
AU - Nomoto, Kikuo
N1 - Funding Information:
This work was supported by a Grant-in-Aid for Scientific Reseach from the ministry of Education, Science and Culture, Japan. We thank Ms. Shigeko Ueda, Ms. Chikako Ishikawa, Ms. Izumi Ohyama, and Ms. Atsuko Yamada for technical assistance and secretarial help.
PY - 1984
Y1 - 1984
N2 - A humoral factor capable of augmenting antigen-specific DTH has been found in the culture supernaant of immune spleen cells and erythrocyte antigen. In this study, a similar factor was identified in the sera of mice sensitized and elicited with heterologous erythrocytes, and the nature of this factor was investigated. Elicitation with antigen was essentially required for the production of the augmentation factor in sensitized mice. The factor showed antigen specificity and antigen-binding capacity. The activity was not assigned to immunoglobulins, as demonstrated by an absorption test with rabbit anti-mouse immunoglobulin-conjugated Sepharose. The activity was stable to heating at 56°C for 30 min, to changes of pH from 3 to 10, and to treatment with trypsin or neuraminidase. The molecular weight of this factor was about 200,000 to 450,000.
AB - A humoral factor capable of augmenting antigen-specific DTH has been found in the culture supernaant of immune spleen cells and erythrocyte antigen. In this study, a similar factor was identified in the sera of mice sensitized and elicited with heterologous erythrocytes, and the nature of this factor was investigated. Elicitation with antigen was essentially required for the production of the augmentation factor in sensitized mice. The factor showed antigen specificity and antigen-binding capacity. The activity was not assigned to immunoglobulins, as demonstrated by an absorption test with rabbit anti-mouse immunoglobulin-conjugated Sepharose. The activity was stable to heating at 56°C for 30 min, to changes of pH from 3 to 10, and to treatment with trypsin or neuraminidase. The molecular weight of this factor was about 200,000 to 450,000.
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U2 - 10.1016/0008-8749(87)90055-4
DO - 10.1016/0008-8749(87)90055-4
M3 - Article
C2 - 6478513
AN - SCOPUS:84886641202
SN - 0008-8749
VL - 88
SP - 184
EP - 192
JO - Cellular Immunology
JF - Cellular Immunology
IS - 1
ER -