Binding of B Cell - Derived Autocrine Growth Factor to Hemoglobin / 대한면역학회지
Korean Journal of Immunology
;
: 25-30, 1998.
Article
in Korean
| WPRIM
| ID: wpr-90169
ABSTRACT
Normal human B cells produce autocrine growth factor in response to Staphylococcus aureus Cowan I strain (SAC). However, the functional role and molecular nature of the B cell derived-B cell growth factor (B-BCGF) are largely unknown. We have tried to investigate the nature of B-BCGF using mAb for several years. We report here that B- BCGF is capable of binding to hemoglobin (Hb). The concentrated culture supernatant from tonsillar B cells stimulated with SAC for 24 h was loaded into the fast protein liquid chromatography and ion-exchange chromatography. The peak with BCGF activity was shown to have a M.W. of 16-18 Kda in polyacrylamide gel electrophoresis followed by silver stain. Amino acid sequence of the fraction was found to identical to human hemoglobin (Hb) by more than 85%. However, Hb itself had no BCGF activity. The presence of Hb in culture supernatant was due to the contamination of SRBC during B cell purification. SRSC were completely removed from B cells by percoll-gradient centrifugation and B cells were stimulated with SAC and exogenous Hb was added to the cultures. The Hb fraction from FPLC again showed a BCGF activity. These data strongly suggested that BCGF binds to Hb. We confirmed this in dot blot as well as Western blot. The M.W of Hb-binding BCGF was 20 Kda. This information may provide a rapid progress in research of BCGF.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Silver
/
Staphylococcus aureus
/
B-Lymphocytes
/
Centrifugation
/
Blotting, Western
/
Chromatography, Ion Exchange
/
Chromatography, Liquid
/
Amino Acid Sequence
/
Electrophoresis, Polyacrylamide Gel
Limits:
Humans
Language:
Korean
Journal:
Korean Journal of Immunology
Year:
1998
Type:
Article
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