Characterization of the murine corticosteroid binding globulin: Variations between mammalian forms
| ISSN: |
0022-4731
|
|---|---|
| Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
|
| Topics: |
Biology
Chemistry and Pharmacology
|
| Type of Medium: |
Electronic Resource
|
| URL: |
| _version_ | 1798291103262179330 |
|---|---|
| autor | Nyberg, L. Marekov, L.N. Jones, I. Lundquist, G. Jornvall, H. |
| autorsonst | Nyberg, L. Marekov, L.N. Jones, I. Lundquist, G. Jornvall, H. |
| book_url | http://linkinghub.elsevier.com/retrieve/pii/0022-4731(90)90146-J |
| datenlieferant | nat_lic_papers |
| fussnote | Corticosteroid binding globulin (CBG) from term-pregnant mouse serum was isolated and characterized by peptide analysis after treatment with CNBr and Lys-specific protease, respectively. Amino acid sequence analysis of six segments, covering 189 of 383 positions in different regions of the protein, showed unexpectedly low overall homology (60%) to the indirectly deduced human amino acid sequence previously reported. However, some segments displayed a greater resemblance to their human counterparts. Differences were observed in at least two of six potential glycosylation sites. The nature of electrophoretic CBG variants and their immunological properties are described. |
| hauptsatz | hsatz_simple |
| identnr | NLZ186335377 |
| issn | 0022-4731 |
| journal_name | Journal of Steroid Biochemistry |
| materialart | 1 |
| package_name | Elsevier |
| publikationsort | Amsterdam |
| publisher | Elsevier |
| reference | 35 (1990), S. 61-65 |
| search_space | articles |
| shingle_author_1 | Nyberg, L. Marekov, L.N. Jones, I. Lundquist, G. Jornvall, H. |
| shingle_author_2 | Nyberg, L. Marekov, L.N. Jones, I. Lundquist, G. Jornvall, H. |
| shingle_author_3 | Nyberg, L. Marekov, L.N. Jones, I. Lundquist, G. Jornvall, H. |
| shingle_author_4 | Nyberg, L. Marekov, L.N. Jones, I. Lundquist, G. Jornvall, H. |
| shingle_catch_all_1 | Nyberg, L. Marekov, L.N. Jones, I. Lundquist, G. Jornvall, H. Characterization of the murine corticosteroid binding globulin: Variations between mammalian forms 0022-4731 00224731 Elsevier |
| shingle_catch_all_2 | Nyberg, L. Marekov, L.N. Jones, I. Lundquist, G. Jornvall, H. Characterization of the murine corticosteroid binding globulin: Variations between mammalian forms 0022-4731 00224731 Elsevier |
| shingle_catch_all_3 | Nyberg, L. Marekov, L.N. Jones, I. Lundquist, G. Jornvall, H. Characterization of the murine corticosteroid binding globulin: Variations between mammalian forms 0022-4731 00224731 Elsevier |
| shingle_catch_all_4 | Nyberg, L. Marekov, L.N. Jones, I. Lundquist, G. Jornvall, H. Characterization of the murine corticosteroid binding globulin: Variations between mammalian forms 0022-4731 00224731 Elsevier |
| shingle_title_1 | Characterization of the murine corticosteroid binding globulin: Variations between mammalian forms |
| shingle_title_2 | Characterization of the murine corticosteroid binding globulin: Variations between mammalian forms |
| shingle_title_3 | Characterization of the murine corticosteroid binding globulin: Variations between mammalian forms |
| shingle_title_4 | Characterization of the murine corticosteroid binding globulin: Variations between mammalian forms |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
| timestamp | 2024-05-06T08:27:18.115Z |
| titel | Characterization of the murine corticosteroid binding globulin: Variations between mammalian forms |
| titel_suche | Characterization of the murine corticosteroid binding globulin: Variations between mammalian forms Corticosteroid binding globulin (CBG) from term-pregnant mouse serum was isolated and characterized by peptide analysis after treatment with CNBr and Lys-specific protease, respectively. Amino acid sequence analysis of six segments, covering 189 of 383 positions in different regions of the protein, showed unexpectedly low overall homology (60%) to the indirectly deduced human amino acid sequence previously reported. However, some segments displayed a greater resemblance to their human counterparts. Differences were observed in at least two of six potential glycosylation sites. The nature of electrophoretic CBG variants and their immunological properties are described. |
| topic | W V |
| uid | nat_lic_papers_NLZ186335377 |