Formation and ultrastructure of enzymically active polymers of pig renal glutaminase |
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| Authors: | B R Olsen G Svenneby E Kvamme B Tveit T Eskeland |
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| Affiliation: | 1. Department of Immunology and Infectious Disease, The Forsyth Institute, Cambridge, MA, USA;2. Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark;3. Department of Developmental Biology, Harvard School of Dental Medicine, Boston, MA, USA;2. Marquette University, Milwaukee, WI, United States |
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| Abstract: | Highly purified pig renal glutaminase has been subjected to electron microscopy. It is shown that the polymers formed after addition of phosphate-borate to enzyme dissolved in Tris-HCl buffer consist of long, double-stranded helices. Addition of phosphate to the Tris-HCl form of the enzyme probably induces the formation of dimers of the Tris-HCl units. It is further demonstrated that the rate of formation of the phosphate form and phosphate-borate form from Tris-HCl units, closely follows the increase in the catalytic activity of the enzyme. |
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