חיפוש מתקדם
Biochemistry (source )
Ilan, E., Department of Bio-medical Engineering, Technion, Haifa 32000, Israel
Avissar, I., Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Tel-Aviv 69978, Israel
Banin, D., Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Tel-Aviv 69978, Israel
Daniel, E., Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Tel-Aviv 69978, Israel
Hemocyanin from the terrestrial snail Levantina hierosolima (Gastropoda, Pulmonata) was studied. A Mw of 10.4 × 106 was determined for the native 100S molecule by sedimentation equilibrium. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis gave one band with a mobility corresponding to a Mw of 360 000. The molecular weight of the polypeptide chain was determined to be 334 000 by sedimentation equilibrium in 6 M guanidine hydrochloride and 0.1 M 2-mercaptoethanol. Analysis of the copper content gave 0.229%, corresponding to a minimal weight per two copper atoms of 55 000. We conclude that a 100S molecule of Levantina hemocyanin is composed of 30 polypeptide chains, each of which contains six binuclear copper centers for binding oxygen. These findings constitute a fundamental departure from the 20 polypeptide chain eight functional unit model currently accepted for gastropod 100S hemocyanin. © 1986 American Chemical Society.
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תנאי שימוש
Subunit structure of hemocyanin from the gastropod Levantina hierosolima
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Ilan, E., Department of Bio-medical Engineering, Technion, Haifa 32000, Israel
Avissar, I., Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Tel-Aviv 69978, Israel
Banin, D., Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Tel-Aviv 69978, Israel
Daniel, E., Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Tel-Aviv 69978, Israel
Subunit structure of hemocyanin from the gastropod Levantina hierosolima
Hemocyanin from the terrestrial snail Levantina hierosolima (Gastropoda, Pulmonata) was studied. A Mw of 10.4 × 106 was determined for the native 100S molecule by sedimentation equilibrium. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis gave one band with a mobility corresponding to a Mw of 360 000. The molecular weight of the polypeptide chain was determined to be 334 000 by sedimentation equilibrium in 6 M guanidine hydrochloride and 0.1 M 2-mercaptoethanol. Analysis of the copper content gave 0.229%, corresponding to a minimal weight per two copper atoms of 55 000. We conclude that a 100S molecule of Levantina hemocyanin is composed of 30 polypeptide chains, each of which contains six binuclear copper centers for binding oxygen. These findings constitute a fundamental departure from the 20 polypeptide chain eight functional unit model currently accepted for gastropod 100S hemocyanin. © 1986 American Chemical Society.
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