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- W1607132615 abstract "Conditions of pH and NaCl concentration were established whereby highly purified Fraction-I protein was crystallized. Identity of the crystalline material with Fraction-I protein was shown by ultraviolet absorption, analytical centrifugation, immunological properties, and Sephadex chromatography. The specific ribulose diphosphate carboxylase6 (3-phospho-d-glycerate carboxy-lyase (EC 4.1.1.39)) activity of crystallized Fraction-I protein was higher than either the purified Fraction-I protein used for crystallization or the protein which remained dissolved in the mother liquor. The crystals are composed of 12 faces, each being parallelograms, united to form 6 apices where 3 faces are joined and 8 apices where 4 faces are joined. The crystals show little birefringence. A model corresponding to the appearance of the crystals was constructed by combining an octahedron with a cube where 2/√2 was the ratio of the longer to shorter diameter, the angles between faces were 60°, and the acute angle of a face was 70.32° compared to the obtuse angle of 109.68°." @default.
- W1607132615 created "2016-06-24" @default.
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- W1607132615 date "1971-01-01" @default.
- W1607132615 modified "2023-09-24" @default.
- W1607132615 title "Studies on fraction-I protein" @default.
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- W1607132615 doi "https://doi.org/10.1016/0005-2795(71)90339-4" @default.
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