Alteration of isoform of alpha-1-acide glycoprotein at heart failure
| Project/Area Number |
05670585
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Circulatory organs internal medicine
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| Research Institution | HOKKAIDO UNIVERSITY |
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Principal Investigator |
NOMURA Akikazu HOKKAIDO UNIVERSITY,SCHOOL PF MEDICINE,DEPARTMENT OF CARDIOVASCULAAR MEDICINE,LECTURE, 医学部, 講師 (70180776)
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| Co-Investigator(Kenkyū-buntansha) |
IKEDA Ken HOKKAIDO UNIVERSITY,HOKKAIDO UNIVERSITY HOSPITAL,DEPARTMENT OF PHARMACY,ASSISTAN, 医学部・附属病院, 助教授 (40203062)
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| Project Period (FY) |
1993 – 1994
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| Project Status |
Completed (Fiscal Year 1994)
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| Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1994: ¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 1993: ¥800,000 (Direct Cost: ¥800,000)
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| Keywords | Alpha-1-acide glycoprotein / Heart failure / HPLC / Number of binding site / Affinity constant / Suger / スキャッチャード・プロット |
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| Research Abstract |
We developed the isolation method of alpha-1-acid glycoprotein (AAG).AAG concentration in serum became hightest at 4th day after acute myocardial infarction and became to the original level in 2 weeks.Binding of disopyramide, which bind to AAG,was lowest at the 4th day and returnd to the original level in 2 weeks.Then we compared the protein binding characteristics of disopyramide for the isolated AAG of the 4th day and of 4th week.There was no change in dissociation constant between them.However, the number of binding sites was lower in 4th day AAG compared to 4th week one.We also measured the concentration of sugers of AAG.There was no change in fucose concentration between them.However, the concentrations of N-acetylglucosamin, galactose, mannose and N-acetylneuramic acid were higher in 4th day AAG compared to 4th week one.We concluded the constitutional change of AAG influenced the protein binding of the drug.
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Report
(3 results)
Research Products
(10 results)
