Abstract
The complementary DNAs encoding human interferon-γ (IFN-γ) and human interleukin-2 (IL-2), two different proteins involved in the same immune system, were fused to code a hybrid protein, which was expressed in E. coli to investigate the interactions of these two proteins at the molecular level. Through immunoprecipitation analysis, this protein was revealed to be of about 31 kDa, which was expected from nucleotide sequencing, and to have the antigenicities of both IFN-γ and IL-2. The extract from bacteria expressing this hybrid protein showed at least two biological activities: an antiviral activity derived from IFN-γ and the ability to support the growth of natural killer (NK) cells derived from IL-2. Comparing the enhancement of NK cell activity of this hybrid protein with IFN-γ and IL-2, this hybrid protein appears to conserve each activity almost completely without diminishing the other.
| Original language | English |
|---|---|
| Pages (from-to) | 187-192 |
| Number of pages | 6 |
| Journal | FEBS Letters |
| Volume | 199 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Apr 21 1986 |
| Externally published | Yes |
Fingerprint
Keywords
- (Human)
- Antigenicity
- complementary DNA
- Hybrid protein
- Integrated biological activity
- Interferon-γ
- Interleukin-2
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
A hybrid protein between IFN-γ and IL-2. / Seno, Masaharu; Hinuma, Shuji; Onda, Haruo; Igarashi, Koichi.
In: FEBS Letters, Vol. 199, No. 2, 21.04.1986, p. 187-192.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A hybrid protein between IFN-γ and IL-2
AU - Seno, Masaharu
AU - Hinuma, Shuji
AU - Onda, Haruo
AU - Igarashi, Koichi
PY - 1986/4/21
Y1 - 1986/4/21
N2 - The complementary DNAs encoding human interferon-γ (IFN-γ) and human interleukin-2 (IL-2), two different proteins involved in the same immune system, were fused to code a hybrid protein, which was expressed in E. coli to investigate the interactions of these two proteins at the molecular level. Through immunoprecipitation analysis, this protein was revealed to be of about 31 kDa, which was expected from nucleotide sequencing, and to have the antigenicities of both IFN-γ and IL-2. The extract from bacteria expressing this hybrid protein showed at least two biological activities: an antiviral activity derived from IFN-γ and the ability to support the growth of natural killer (NK) cells derived from IL-2. Comparing the enhancement of NK cell activity of this hybrid protein with IFN-γ and IL-2, this hybrid protein appears to conserve each activity almost completely without diminishing the other.
AB - The complementary DNAs encoding human interferon-γ (IFN-γ) and human interleukin-2 (IL-2), two different proteins involved in the same immune system, were fused to code a hybrid protein, which was expressed in E. coli to investigate the interactions of these two proteins at the molecular level. Through immunoprecipitation analysis, this protein was revealed to be of about 31 kDa, which was expected from nucleotide sequencing, and to have the antigenicities of both IFN-γ and IL-2. The extract from bacteria expressing this hybrid protein showed at least two biological activities: an antiviral activity derived from IFN-γ and the ability to support the growth of natural killer (NK) cells derived from IL-2. Comparing the enhancement of NK cell activity of this hybrid protein with IFN-γ and IL-2, this hybrid protein appears to conserve each activity almost completely without diminishing the other.
KW - (Human)
KW - Antigenicity
KW - complementary DNA
KW - Hybrid protein
KW - Integrated biological activity
KW - Interferon-γ
KW - Interleukin-2
UR - http://www.scopus.com/inward/record.url?scp=0022480894&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0022480894&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(86)80477-X
DO - 10.1016/0014-5793(86)80477-X
M3 - Article
C2 - 3009218
AN - SCOPUS:0022480894
VL - 199
SP - 187
EP - 192
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 2
ER -