Simplified Method for Purification of Mouse β1H

التفاصيل البيبلوغرافية
العنوان: Simplified Method for Purification of Mouse β1H
المؤلفون: Toshio Kaidoh, Shunnosuke Natsuume-Sakai, Teizo Fujita, Morinobu Takahashi, Yuko Takata
المصدر: Complement. 1:44-51
بيانات النشر: S. Karger AG, 1984.
سنة النشر: 1984
مصطلحات موضوعية: Gel electrophoresis, Chromatography, medicine.diagnostic_test, biology, Chemistry, Immunology, Size-exclusion chromatography, Hematology, Immunoelectrophoresis, Monospecific antibody, Complement system, Sepharose, Affinity chromatography, medicine, biology.protein, Beta (finance)
الوصف: A simple three-step method was described for purification of murine beta 1H, one of the essential regulatory proteins of complement system. The method consists of heparin-Sepharose affinity chromatography; gel filtration on a Sepharose 6B column, and DNA-cellulose affinity chromatography. By this method over 10 mg of beta 1H can be purified by more than 200-fold from 100-ml of EDTA serum of various strains. Overall yield of beta 1H was about 45%. The purified beta 1H was homogeneous as judged by SDS-polyacrylamide gel electrophoresis and immunoelectrophoresis. The purified mouse beta 1H showed physicochemical properties very similar to those described for human beta 1H: mouse beta 1H is a beta-globulin consisting of a single polypeptide chain of molecular weight of 160,000. Purified mouse beta 1H retained its functional activity as the essential cofactor for the cleavage of fluid-phase human C3b by the human C3b inactivator. Immunization of rabbits with the purified mouse beta 1H resulted in the production of the potent and monospecific antibody.
تدمد: 2504-2424
0253-5076
DOI: 10.1159/000467813
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::b912e0800d9eaeb3a38239b8f8fe48dd
https://doi.org/10.1159/000467813
Rights: CLOSED
رقم الانضمام: edsair.doi...........b912e0800d9eaeb3a38239b8f8fe48dd
قاعدة البيانات: OpenAIRE
الوصف
تدمد:25042424
02535076
DOI:10.1159/000467813