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피조개(Scapharca broughtonii)혈액 ferritin의 철분산화 기작에 관한 연구
손화숙,박충웅,김경숙,Sohn, Hwa-Suk,Park, Chung-Ung,Kim, Kyung-Suk 생화학분자생물학회 1992 한국생화학회지 Vol.25 No.3
혈액내 철분의 농도가 비교적 높은(약 $4,000{\sim}5,000\;{\mu}gFe$/100ml) 피조개(Scaþharca broughtonii) 혈액에서 ferritin을 분리 정제하여 그 특성을 부분적으로 밝히고 ferritin core에 있어서 철분산화 기작을 연구하고자 단백질내 iron-core의 상태 및 성질을 조사하였으며 iron uptake시 초기 반응속도를 측정하였다. 이 단백질의 분자량은 500 kDa으로 산출되었고 subunit는 단일종으로 이루어져 있으며 size가 21 kDa이었다. 분리된 ferritin 분자내 함유된 철분은 평균 1,400~2,000 atoms이었다. Ferritin core의 상태는 전자현미경을 이용하여 ferrihydrite로 추정되었으며 M$\ddot{o}$ssbauer spectroscopy를 이용한 예비실험 결과 특이하게도 $T_{ord}$는 20 K 부근, $T_B$는 13 K보다 낮은 온도였다. 철분 산화반응에 있어서의 초기 반응속도는 Fe(II)의 농도에 비례하였고 단백질의 농도에 대해서도 비례함이 밝혀졌다. We have isolated ferritin from the blood of the marine bivalve mollusc Scapharca broughtonii in which blood iron levels were high (approx. $4,000{\sim}5,000\;{\mu}gFe$/100ml). The blood ferritin had a $M_r$ of ca. 500,000 with a single subunit type having a $M_r$ of ca. 21,000. The isolated ferritin contained 1,400~2,000 atoms Fe/molecule on average. The bivalve ferritin core was examined preliminarily using an electron microscope and its electron diffraction pattern implied characteristic lines of ferrihydrite. The preliminary M$\ddot{o}$ssbauer spectra of the S. broughtonii ferritin showed a striking difference. $T_{ord}$ was estimated ca. 20 K and $T_B$ was lower than 13 K. Ferroxidase activity of the bivalve apoferritin was assayed and characterized. Apoferritin catalyzes the oxidation of Fe(II) to Fe(III). The initial rate of Fe(II) oxidation was dependent on Fe(II) concentration and a linear dependence of initial rate on protein concentration was observed.
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피조개 ( Scapharca broughtonii ) 혈액 ferritin 의 철분산화 기작에 관한 연구
손화숙,박충웅,김경숙 ( Hwa Suk Sohn,Chung Ung Park,Kyung Suk Kim ) 생화학분자생물학회 1992 BMB Reports Vol.25 No.3
We have isolated ferritin from the blood of the marine bivalve mollusc Scapharca broughtonii in which blood iron levels were high (approx. 4,000∼5,000 ㎍Fe/100 ml). The blood ferritin had a M_r of ca. 500,000 with a single subunit type having a M_r of ca. 21,000. The isolated ferritin contained 1,400∼2,000 atoms Fe/molecule on average. The bivalve ferritin core was examined preliminarily using an electron microscope and its electron diffraction pattern implied characteristic lines of ferrihydrite. The preliminary Mo¨ssbauer spectra of the S broughtonii ferritin showed a striking difference. T_(ord) was estimated ca. 20 K and T_B was lower than 13 K. Ferroxidase activity of the bivalve apoferritin was assayed and characterized. Apoferritin catalyzes the oxidation of Fe(II) to Fe(III). The initial rate of Fe(II) oxidation was dependent on Fe(II) concentration and a linear dependence of initial rate on protein concentration was observed.
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