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RISS 인기검색어
- 검색키워드
- 저자 : 장정순 ( Sang Bog Kim (검색결과 6 건)
- 무료
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Swamp eel (Monopterus albus)혈장 Albumin분획의 정제 및 물리화학적 성상에 관한 연구
김상복,장정순,Kim, Sang-Bog,Chang, Chung-Soon 생화학분자생물학회 1982 한국생화학회지 Vol.15 No.4
드렁허리(Monopterus albus)로부터 albumin분획 만을 정제하기 위하여 ammonium sulfate로 crude albumin분획을 얻은 후, 다시 DEAE-Sephadex A-50을 이용한 column chromatography로 albumin분획을 정제하였다. 정제된 albumin분획의 물리화학적 성상을 알기 위하여 organic cation인 rivanol을 이용한 albumin분획의 확인실험, $NaDodSO_4$-PAGE에 의한 분자량 측정, 흡광계수, 침강계수 및 -SH 함량등을 측정하였다. 즉 어류의 혈장으로부터 albumin분획을 분리할때 완만한 구배농도의 증가와 많은 양의 buffer로 유출시켰을 때 정제된 albumin을 얻을 수 있었고 드렁허리 정제 albumin의 분자량은 이미 알려진 다른 동물의 것에 비하여 분자량이 절반 정도였으며 -SH함량도 0.04로 매우낮았다. 끝으로, 흡광계수는 30,320 $mol^{-1}cm^{-1}$이었으며 침강계수는 dimer의 상태일때 4.5 S, neutral sugar의 함량은 대략$39{\pm}0.2{\mu}g$per mg 단백질을 나타내었다. Albumin fraction was purified from the swamp eel by salting out with ammonium sulfate and following by DEAE-Sephadex A50 column chromatography. The purified albumin fraction appeared to be homogeneous by Davis and $NaDodSO_4$ polyacrylamide gel electrophoresis after albumin fraction was treated with organic cation, rivanol (2-ethoxy-6,9, diaminoacridine lactate). The physico-chemical properties on purified albumin fraction were characterized by means of molecular weight determination, -SH content, extinction and sedimentation coefficient, etc.
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Swamp eel ( Monopterus albus ) 혈장 Albumin 분획의 정제 및 물리화학적 성상에 관한 연구
김상복,장정순 ( Sang Bog Kim,Chung Soon Chang ) 생화학분자생물학회 1982 BMB Reports Vol.15 No.4
Albumin fraction was purified from the swamp eel by salting out with ammonium sulfate and following by DEAE-Sephadex A50 column chromatography. The purified albumin fraction appeared to be homogeneous by Davis and NaDodSO₄ polyacrylamide gel electrophoresis after albumin fraction was treated with organic cation, rivanol (2-ethoxy-6, 9, diaminoacridine lactate). The physico-chemical properties on purified albumin fraction were characterized by means of molecular weight determination, -SH content, extinction and sedimentation coefficient, etc.
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김상복,이강석,유병선,장정순,김정규 ( Sang Bog Kim,Kang Suk Lee,Byung Sun Yoo,Chung Soon Chang,Jung Kyu Kim ) 생화학분자생물학회 1993 BMB Reports Vol.26 No.6
A high molecular weight proteinase inhibitor has been purified from the body fluid of sea crab (Portunus trituberculatus) using biospecific Zn^(2+) chelate affinity chromatography. The proteinase inhibitor inhibits the proteolytic activity of a variety of endopeptidase such as trypsin, chymotrypsin and thermolysin. Like other vertebrate α-M, the sea crab α-macroglobulin (α-M) was composed of subunits of molecular weight 180 kDa as judged by polyacrylamide gel electrophoresis under reducing conditions. The apparent native molecular weight of the sea crab α-M determined by gel filtration was 360 kDa. Thermal fragmentation studies revealed that the monomer (180 kDa) was broken down into 95 kDa and 85 kDa fragments, respectively. On the basis of above results, it is concluded that the sea crab α-M is a dimer consisting of two weakly bound monomer,and the autolytic cleavage occurs easily by SDS and heat treatment.
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김상복,이강석,김인규,유병선,장정순,Kim, Sang-Bog,Lee, Kang-Suk,Kim, In-Kyu,Yoo, Byung-Sun,Chang, Chung-Soon 생화학분자생물학회 1993 한국생화학회지 Vol.26 No.8
꽃게(Portunus trituberculatus) 체액에서 정제된 ${\alpha}$-macroglobulin(${\alpha}$-M)은 단백질 분해억제물질로 고등동물의 ${\alpha}_2$-M과는 달리 trypsin과의 결합비는 casein 및 TAME를 기질로 사용하였을 때 1:0.3으로 닭, 개구리(Rana pipiens), 바다가재(Hamarus americanus) 등 보다 낮은 값을 나타냄으로써 하등으로 내려갈수록 trypsin과의 결합비가 점차 낮아진다는 사실을 알수 있었다. 한편 꽃게 ${\alpha}$-M을 methylamine으로 변성시킬 경우 trypsin의 활성은 억제되지 않았으며, 이러한 결과는 지금까지 밝혀진 척추 및 무척추동물의 ${\alpha}_2$-M 의 생화학적 특성과 일치하였다. 꽃게 ${\alpha}$-M의 아미노산 조성을 지금까지 밝혀진 다른 동물의 ${\alpha}_2$-M과 비교한 결과 aspartic acid의 함량이 다소 높은 것을 제외하고는 대부분의 아미노산 조성이 서로 비슷한 경향을 보였다. 이러한 꽃게 ${\alpha}$-M의 아미노산 조성을 근거로 $S{\Delta}Q$값을 사용하여 단백질의 근연관계를 조사한 결과 꽃게 ${\alpha}$-M은 개구리, 투구게(Limulus polyphemus)의 ${\alpha}$-M과 매우 가까운 단백질로 밝혀졌다. Trypsin binding studies showed that sea crab ${\alpha}$-macroglobulin (${\alpha}$-M) could bind 0.3 mol of trypsin per molecule. It can, therefore, be concluded that the molecular ratio of proteinase/inhibitor was different from the stoichiometry for human ${\alpha}_2$-M (half molecule) and also different from other data for the southern grass frog and American lobster where the values were in the range of 0.45~0.79 mol of trypsin/mol of macroglobulin, indicating the lower animals showed low trypsin binding capacity compared with that of higher animals. The ${\alpha}$-M of the sea crab completely lost its ability for inhibition of trypsin activity by methylamine. The analysis of $S{\Delta}Q$ parameter based on the amino acid compositions indicated that the sea crab ${\alpha}$-M is closely related with that of the frog (Rana pipiens) and the horseshoe crab, respectively.
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김상복,이강석,유병선,장정순,김정규,Kim, Sang-Bog,Lee, Kang-Suk,Yoo, Byung-Sun,Chang, Chung-Soon,Kim, Jung-Kyu 생화학분자생물학회 1993 한국생화학회지 Vol.26 No.6
꽃게(Portunus trituberculatus) 체액을 $Zn^{2+}$ -chelate affinity column을 이용하여 분리 정제하였다. 그 결과 척추동물의 경우와는 달리 affinity gel의 재생과정($Zn^{2+}$ 이온제거)인 50mM EDTA(ethylene diaminetetraacetic acid) 분획에서 ${\alpha}-macroglobulin({\alpha}-M)$이 분리되였다. 꽃게의 ${\alpha}-macroglobulin$은 trypsin, chymotrypsin, thermolysin의 활성을 억제하였으나, 사람의 ${\alpha}_{2}-macroglobulin$과는 달리 subtilisin과 cathepsin C 등의 활성은 억제하지 못하였다. 또한 고등동물의 경우와 달리 trypsin 보다는 thermolysin과의 친화력이 높았다. 꽃게 ${\alpha}-M$은 monomer의 분자량이 180 kDa인 dimer의 행태로 존재하며 상기 monomer는 열과 detergent(SDS)에 의해서 분자량 95 kDa 및 85 kDa의 polypeptide로 분리되었다. A high molecular weight proteinase inhibitor has been purified from the body fluid of sea crab (Portunus trituberculatus) using biospecific $Zn^{2+}$ chelate affinity chromatography. The proteinase inhibitor inhibits the proteolytic activity of a variety of endopeptidase such as trypsin, chymotrypsin and thermolysin. Like other vertebrate ${\alpha}-M$, the sea crab ${\alpha}-macroglobulin$ $({\alpha}-M)$ was composed of subunits of molecular weight 180 kDa as judged by polyacrylamide gel electrophoresis under reducing conditions. The apparent native molecular weight of the sea crab ${\alpha}-M$ determined by gel filtration was 360 kDa. Thermal fragmentation studies revealed that the monomer (180 kDa) was broken down into 95 kDa and 85 kDa fragments, respectively. On the basis of above results, it is concluded that the sea crab ${\alpha}-M$ is a dimer consisting of two weakly bound monomer,and the autolytic cleavage occurs easily by SDS and heat treatment.
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김상복,이강석,김인규,유병선,장정순 ( Sang Bog Kim,Kang Suk Lee,In Kyu Kim,Byung Sun Yoo,Chung Soon Chang ) 생화학분자생물학회 1993 BMB Reports Vol.26 No.8
Trypsin binding studies showed that sea crab α-macroglobulin (α-M) could bind 0.3 ㏖ of trypsin per molecule. It can, therefore, be concluded that the molecular ratio of proteinase/inhibitor was different from the stoichiometry for human α₂-M (half ㏖ecule) and also different from other data for the southern grass frog and American lobster where the values were in the range of 0.45∼0.79 ㏖ of trypsin/㏖ of macroglobulin, indicating the lower animals showed low trypsin binding capacity compared with that of higher animals. The a-M of the sea crab completely lost its ability for inhibition of trypsin activity by methylamine. The analysis of SΔQ parameter based on the amino acid compositions indicated that the sea crab α-M is closely related with that of the frog (Rana pipiens) and the horseshoe crab, respectively.
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