A partially purified membrane protein specific to the brain
| ISSN: |
0005-2795
|
|---|---|
| Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
|
| Topics: |
Biology
|
| Type of Medium: |
Electronic Resource
|
| URL: |
| _version_ | 1798292385589886978 |
|---|---|
| autor | Lim, R. Goedken, M.P. |
| autorsonst | Lim, R. Goedken, M.P. |
| book_url | http://linkinghub.elsevier.com/retrieve/pii/0005-2795(73)90311-5 |
| datenlieferant | nat_lic_papers |
| fussnote | A brain-specific protein was partially purified from the particulate fraction of the cerebral cortex by dissociation with lithium diiodosalicylate, phenol treatment and ethanol precipitation. The product was water-soluble and showed several bands on polyacrylamide electrophoresis. Only one of these bands showed antigenic activity. The antigenicity was destroyed by trypsin but not by deoxyribonuclease, ribonuclease, neuraminidase or periodate oxidation. The antigen was not precipitable by vinblastine. The antiserum against this protein did not cross-react with S-100 protein, the myelin basic protein, and the liver membrane proteins. The immunological activity of the serum toward the brain protein was not affected by adsorption with membranes from liver, kidney and muscle, but was completely abolished after adsorption with cerebral membranes. The protein antigen was sensitive to acid but resistant to alkali. At physiological pH it was heat-stable. In contrast to most proteins, the protein band took up a pink color rather than blue when stained with Coomassie brilliant blue. The antigen had a molecular weight of 42 000 and appeared to consist of dissociable subunits. |
| hauptsatz | hsatz_simple |
| identnr | NLZ186075391 |
| issn | 0005-2795 |
| journal_name | BBA - Protein Structure |
| materialart | 1 |
| package_name | Elsevier |
| publikationsort | Amsterdam |
| publisher | Elsevier |
| reference | 322 (1973), S. 359-371 |
| search_space | articles |
| shingle_author_1 | Lim, R. Goedken, M.P. |
| shingle_author_2 | Lim, R. Goedken, M.P. |
| shingle_author_3 | Lim, R. Goedken, M.P. |
| shingle_author_4 | Lim, R. Goedken, M.P. |
| shingle_catch_all_1 | Lim, R. Goedken, M.P. A partially purified membrane protein specific to the brain 0005-2795 00052795 Elsevier |
| shingle_catch_all_2 | Lim, R. Goedken, M.P. A partially purified membrane protein specific to the brain 0005-2795 00052795 Elsevier |
| shingle_catch_all_3 | Lim, R. Goedken, M.P. A partially purified membrane protein specific to the brain 0005-2795 00052795 Elsevier |
| shingle_catch_all_4 | Lim, R. Goedken, M.P. A partially purified membrane protein specific to the brain 0005-2795 00052795 Elsevier |
| shingle_title_1 | A partially purified membrane protein specific to the brain |
| shingle_title_2 | A partially purified membrane protein specific to the brain |
| shingle_title_3 | A partially purified membrane protein specific to the brain |
| shingle_title_4 | A partially purified membrane protein specific to the brain |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
| timestamp | 2024-05-06T08:47:40.767Z |
| titel | A partially purified membrane protein specific to the brain |
| titel_suche | A partially purified membrane protein specific to the brain A brain-specific protein was partially purified from the particulate fraction of the cerebral cortex by dissociation with lithium diiodosalicylate, phenol treatment and ethanol precipitation. The product was water-soluble and showed several bands on polyacrylamide electrophoresis. Only one of these bands showed antigenic activity. The antigenicity was destroyed by trypsin but not by deoxyribonuclease, ribonuclease, neuraminidase or periodate oxidation. The antigen was not precipitable by vinblastine. The antiserum against this protein did not cross-react with S-100 protein, the myelin basic protein, and the liver membrane proteins. The immunological activity of the serum toward the brain protein was not affected by adsorption with membranes from liver, kidney and muscle, but was completely abolished after adsorption with cerebral membranes. The protein antigen was sensitive to acid but resistant to alkali. At physiological pH it was heat-stable. In contrast to most proteins, the protein band took up a pink color rather than blue when stained with Coomassie brilliant blue. The antigen had a molecular weight of 42 000 and appeared to consist of dissociable subunits. |
| topic | W |
| uid | nat_lic_papers_NLZ186075391 |