Starch Phosphorylase of Potato
نویسنده
چکیده
Cori and his colleagues (l-6) discovered and elucidated the series of reversible chemical reactions by which glucose is transformed into glycogen in animal tissues. These reactions are catalyzed by a group of enzymes, the most fundamental of which is phosphorylase, the enzyme which catalyzes the condensation of glucose-l-phosphate (Cori ester) to starch or glycogen. The properties of phosphorylase from animal sources have been systematically investigated by Cori et al. (l-5), while Hanes (7, 8) discovered a similar enzyme in extracts from pea and potato, and made a thorough study of the crude potato enzyme. The present investigation deals with the preparation and some of the characteristics of purified potato phosphorylase.
منابع مشابه
Starch phosphorylase inhibitor from sweet potato.
A protein, starch phosphorylase inhibitor, was purified from the root of sweet potato (Ipomoea batatas [L.] Lam. cv Tainon 65). It had a molecular weight of 250,000 and could be composed of five identical subunits. The isoelectric point of the inhibitor was 4.63. It was a noncompetitive inhibitor toward the sweet potato enzyme with a K(i) value of 1.3 x 10(-6) molar when glucose-1-P was the var...
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متن کاملMaturation and subcellular compartmentation of potato starch phosphorylase.
The subcellular localization and maturation of starch phosphorylase (EC 2.4.1.1) was studied in developing potato tubers. The enzyme is localized inside the stroma of amyloplasts in young tubers, whereas in mature tubers it is found within the cytoplasm in the immediate vicinity of the plastids. A phosphorylase cDNA clone was isolated and used in RNA gel blot experiments to demonstrate that pho...
متن کاملRegulation of the catalytic behaviour of L-form starch phosphorylase from sweet potato roots by proteolysis.
Starch phosphorylase (SP) is an enzyme used for the reversible phosphorolysis of the alpha-glucan in plant cells. When compared to its isoform in an animal cell, glycogen phosphorylase, a peptide containing 78 amino acids (L78) is inserted in the centre of the low-affinity type starch phosphorylase (L-SP). We found that the amino acid sequence of L78 had several interesting features including t...
متن کاملPlastidial Starch Phosphorylase in Sweet Potato Roots Is Proteolytically Modified by Protein-Protein Interaction with the 20S Proteasome
Post-translational regulation plays an important role in cellular metabolism. Earlier studies showed that the activity of plastidial starch phosphorylase (Pho1) may be regulated by proteolytic modification. During the purification of Pho1 from sweet potato roots, we observed an unknown high molecular weight complex (HX) showing Pho1 activity. The two-dimensional gel electrophoresis, mass spectr...
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تاریخ انتشار 2003