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Role of Sialic Acid in the Conformational Change of Serum Haptoglobin by Hemoglobin Binding
윤창수,심봉섭,Yoon, Chang-Soo,Shim, Bong-Sop 생화학분자생물학회 1968 한국생화학회지 Vol.1 No.2
neuramindase로 처리한 1-1형 혈청 haptoglobin의 면역학적 반응성을 토끼의 특이 항-haptoglobin 혈청 및 항-$\beta$-chain 혈청으로 검색하였다. 항-haptoglobin 혈청에 대하여서는 sialic acid를 제거한거나 안한것 간에 항원성에 차이가 없었다. 한편 항-$\beta$-chain 혈청에 대하여서는 sialic acid를 제거하지 않은 1-1형 haptoglobin-hemoglobin 복합체는 반응하지 않았으나 sialic aicd를 제거한 1-1형 haptoglobin-hemoglobin 복합체는 혈색소와 결합한 변이형 haptoglobin Marburg와 마찬가지로 반응하였다. 1967년 Shim 등 (Proc. Soc. Exp. Bol. Med. 126, 221)은 이미 면역학적 방법으로 변이 haptoglobin Marburg는 혈색소와 결합하더라도 정상 haptoglobin 같이 형태의 변화를 초래하지 않는다는 것을 입증한 바 있다. 따라서 혈청 haptoglobin이 혈색소와 결합할 때 형태변화를 일으키는데 있어서 sialic acid가 매우 중요한 역할을 한다고 볼 수 있다. The immunologic reactivities of neuraminidase treated haptoglobin 1-1 type serum was examined with specific rabbit anti-haptoglobin serum and with antiserum to beta-chain of haptoglobin. Sialic acid removed hemoglobin complexed 1-1 type haptoglobin reacted against anti beta-chain serum like hemoglobin complexed haptoglobin "Marburg", while the control hemoglobin complexed 1-1 type haptoglobin did not react. It was demonstrated by Shim et al. (1967) (Proc. Soc. Exp. Bioi. Med. 126, 221) that the variant haptoglobin "Marburg" does not undergo conformational change by hemoglobin binding while normal haptoglobin does. From these facts it was concluded that sialic acid might play an important role in the conformational change of normal haptoglobin by hemoglobin binding.
혈색소와의 결합에 인하는 혈청 Haptoglobin 의 형태변화에 미치는 Sialic Acid 의 영향
윤창수,심봉섭 한국생화학회 1968 BMB Reports Vol.1 No.2
The immunologic reactivities of neuraminidase treated haptoglobin 1-1 type serum was examined with specific rabbit anti-haptoglobin serum and with antiserum to beta-chain of haptoglobin. Sialic acid removed hemoglobin complexed 1-1 type haptoglobin reacted against anti-beta-chain serum like hemoglobin complexed haptoglobin $quot;Marburg$quot;, while the control hemoglobin complexed 1-1 type haptoglobin did not react. It was demonstrated by Shim et al. (1967) (Proc. Soc. Exp. Biol. Med. 126, 221) that the variant haptoglobin $quot;Marburg$quot; does not undergo conformational change by hemoglobin binding while normal haptoglobin does. From these facts it was concluded that sialic acid might play an important role in the conformational change of normal haptoglobin by hemoglobin binding.
Studies on Swine Serum Haptoglobin
윤창수,심봉섭,강윤세,이동호 생화학분자생물학회 1973 BMB Reports Vol.3 No.2
1. Swine serum haptoglobin was purified by DEAE-cellulose chromatography. starch block electrophoresis and finally by gel filtration. 2. The solubilty of swine serum haptoglobin was slightly higher than human type 1-1 haptoglobin, i. e., it precipitated 65 percent saturation of ammonium sulfate. 3. The electrophoretic mobility of swine serum haptogtobin is slower than human type 1-1 haptoglobin and retardation of mobility of swine haptoglobin by forming hemoglobin complex was very slight. For this reason, in starch gel electrophoresis swine Hp-Hb complex migrated faster than human type 1-1 Hp-Hb complex. 4. Swine serum haptoglobin also forms so-called Hp-Hb intermediate as well as human haptoglobin. However, it is difficult to demonstrate by ordinary starch gel electrophoresis, since retardation of mobility of swine haptoglobin by formation of Hp-Hb complex is very slight. 5. Some antigenic determinants of swine serum haptoglobin are masked by hemoglobinbinding. 6. It was found that the molecular weight of swine serum haptoglobin is similar to humar type 1-1 haptoglobin, i. e., around 89, 000, by gel filtration technique. 7. Swine serun haptoglobin is composed of two kinds of polypeptide chains. 1'he smaller alpha-chain was similar to human alpha^(IS)-chain, and the larger beta-chain was similar to human beta-chain The subunit structure of swine haptoglobin is α₂β₂. 8. Swine serum haptoglobin binds with hemoglobin at the beta-chain like human haptoglobin. 9. The swine Hp-Hb complex is composed of equimolar haptoglobin and hemoglobin, while Hp-Hb intermediate is composed of one molecule of haptoglobin and half-molecule (dimer) of hemoglobin.