Gel filtration과 ion exchange chromatography, reversed-phase 및 ion exchange FPLC를 이용하여 고려인삼 뿌리에서 subunit 분자량 약 25 kDa의 주요단백질(이하 GMP)을 분리하였다. PAS 염색을 통하여 GMP는 carbohydrate moiety를 갖는 당단백질일 가능성을 보여주었고, 이는 glycosidase 처리후 protein band shift 실험으로 확인되었다. GMP는 native polyacrylamide 전기영동 및 gel permeation FPLC를 통해 native form은 약 63 kDa의 분자량을 갖는 dimer로 판단된다. GMP의 생리활성 측정결과, inflammation mediator의 기능탐색에 쓰이는 anticomplementary activity를 보여주었다.
The major protein (GMP) from the roots of Panax ginseng C. A. Meyer was purified, using gel filtration and ion exchange chromatography followed by reversed-phase and ion exchange FPLC. Staining analysis indicated that the protein has a carbohydrate moiety, which was also shown by band shift experiments using various glycosidases. Electrophoretic and gel permeation studies showed that GMP has an apparent molecular weight of 63 kDa composed of possibly two subunits of 25 kDa containing carbohydrate moiety. GMP showed an anticomplementary activity on the hemolysis of red blood cells, which is a screening tool for inflammation mediator search.
