Structural relationship between α1-microglobulin from man, guinea-pig, rat and rabbit
(1988) In European Journal of Biochemistry 170(1-2). p.143-148- Abstract
Rabbit α1-microglobulin was purified from the urine of sodium-chromate-treated animals by the use of gel chromatography on Sephadex G-100 affinity chromatography on concanavalin-A - Sepharose and ion-exchange chromatography on DEAE-Sephadex. Rabbit α1-microglobulin had a molecular mass of 25.6 kDa on SDS/polyacrylamide gel electrophoresis. α1-microglobulin has previously been purified from the urine of humans, guinea-pigs and rats by similar methods, and the molecular masses of the four homologues were compared by SDS/polyacrylamide gel electrophoresis and gel chromatography in a denaturing medium. By these two methods the human homologue was 6 kDa and 3 kDa larger, respectively, than the other three... (More)
Rabbit α1-microglobulin was purified from the urine of sodium-chromate-treated animals by the use of gel chromatography on Sephadex G-100 affinity chromatography on concanavalin-A - Sepharose and ion-exchange chromatography on DEAE-Sephadex. Rabbit α1-microglobulin had a molecular mass of 25.6 kDa on SDS/polyacrylamide gel electrophoresis. α1-microglobulin has previously been purified from the urine of humans, guinea-pigs and rats by similar methods, and the molecular masses of the four homologues were compared by SDS/polyacrylamide gel electrophoresis and gel chromatography in a denaturing medium. By these two methods the human homologue was 6 kDa and 3 kDa larger, respectively, than the other three proteins. Endoglycosidase F digestion of α1-microglobulin, followed by SDS/polyacrylamide gel electrophoresis, revealed three protein bands in the human α1-microglobulin sample, and only two bands in guinea-pig, rat and rabbit α1-microglobulin, with a gap between each band of 2.6-2.9 kDa. The amino-terminal amino acid sequences of the four homologues were determined and between 72% and 81% homology was seen. The five amino-terminal amino acids present in the other species were missing in guinea-pig α1-microglobulin. Our results indicate that human α1-microglobulin is substituted with two N-linked oligosaccharides, while only one is attached to each of the other α1-microglobulins, and that the extra glycosylamine-linked oligosaccharide in the human protein is attached to asparagine in position 17. Finally it is shown that all four homologues inhibit antigen stimulation of human lymphocytes, a finding which is consistent with our previous suggestion that the N-linked oligosaccharides carry the immunosuppressive activity of α1-microglobulin.
(Less)
- author
- Akerstrom, B. LU ; Logdberg, L. ; Babiker-Mohammed, H. ; Lohmander, S. LU and Rask, L.
- organization
- publishing date
- 1988
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- α1-microglobulin, animals
- in
- European Journal of Biochemistry
- volume
- 170
- issue
- 1-2
- pages
- 6 pages
- publisher
- Wiley-Blackwell
- external identifiers
-
- pmid:2446872
- scopus:0023870569
- ISSN
- 0014-2956
- language
- English
- LU publication?
- yes
- id
- 04be53b7-43d8-4808-94c2-112cfd964831
- date added to LUP
- 2016-05-04 12:59:34
- date last changed
- 2024-01-04 02:43:03
@article{04be53b7-43d8-4808-94c2-112cfd964831, abstract = {{<p>Rabbit α<sub>1</sub>-microglobulin was purified from the urine of sodium-chromate-treated animals by the use of gel chromatography on Sephadex G-100 affinity chromatography on concanavalin-A - Sepharose and ion-exchange chromatography on DEAE-Sephadex. Rabbit α<sub>1</sub>-microglobulin had a molecular mass of 25.6 kDa on SDS/polyacrylamide gel electrophoresis. α<sub>1</sub>-microglobulin has previously been purified from the urine of humans, guinea-pigs and rats by similar methods, and the molecular masses of the four homologues were compared by SDS/polyacrylamide gel electrophoresis and gel chromatography in a denaturing medium. By these two methods the human homologue was 6 kDa and 3 kDa larger, respectively, than the other three proteins. Endoglycosidase F digestion of α<sub>1</sub>-microglobulin, followed by SDS/polyacrylamide gel electrophoresis, revealed three protein bands in the human α<sub>1</sub>-microglobulin sample, and only two bands in guinea-pig, rat and rabbit α<sub>1</sub>-microglobulin, with a gap between each band of 2.6-2.9 kDa. The amino-terminal amino acid sequences of the four homologues were determined and between 72% and 81% homology was seen. The five amino-terminal amino acids present in the other species were missing in guinea-pig α<sub>1</sub>-microglobulin. Our results indicate that human α<sub>1</sub>-microglobulin is substituted with two N-linked oligosaccharides, while only one is attached to each of the other α<sub>1</sub>-microglobulins, and that the extra glycosylamine-linked oligosaccharide in the human protein is attached to asparagine in position 17. Finally it is shown that all four homologues inhibit antigen stimulation of human lymphocytes, a finding which is consistent with our previous suggestion that the N-linked oligosaccharides carry the immunosuppressive activity of α<sub>1</sub>-microglobulin.</p>}}, author = {{Akerstrom, B. and Logdberg, L. and Babiker-Mohammed, H. and Lohmander, S. and Rask, L.}}, issn = {{0014-2956}}, keywords = {{α1-microglobulin; animals}}, language = {{eng}}, number = {{1-2}}, pages = {{143--148}}, publisher = {{Wiley-Blackwell}}, series = {{European Journal of Biochemistry}}, title = {{Structural relationship between α1-microglobulin from man, guinea-pig, rat and rabbit}}, volume = {{170}}, year = {{1988}}, }