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The purification and properties of a hexokinase from the corn scutellum

Author: Herbert Charles Jones
Publisher: 1965.
Dissertation: Thesis (Ph. D.)--University of Florida, 1965.
Edition/Format:   Thesis/dissertation : Thesis/dissertation : Manuscript   Archival Material : EnglishView all editions and formats
Database:WorldCat
Summary:
The properties of plant enzymes, especially those of higher plants, are less veil known than those of similar enzymes isolated from animal tissues. It has been assumed that the properties associated with the characterized animal and lover plant (yeast) enzymes are the same for higher plants. This may be the case, but it is necessary that the plant enzymes be characterized in order to gain a better understanding of  Read more...
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Additional Physical Format: Online version:
Jones, Herbert Charles, 1936-
Purification and properties of a hexokinase from the corn scutellum.
1965
(OCoLC)820088431
Material Type: Thesis/dissertation, Manuscript
Document Type: Book, Archival Material
All Authors / Contributors: Herbert Charles Jones
OCLC Number: 37463284
Notes: Typescript.
Vita.
Description: vi, 90 leaves : ill. ; 28 cm.
Responsibility: by Herbert Charles Jones.

Abstract:

The properties of plant enzymes, especially those of higher plants, are less veil known than those of similar enzymes isolated from animal tissues. It has been assumed that the properties associated with the characterized animal and lover plant (yeast) enzymes are the same for higher plants. This may be the case, but it is necessary that the plant enzymes be characterized in order to gain a better understanding of the similarities and differences in metabolism between plants and animals. The enzyme, hexokinase, which catalyzes the phosphorylation of glucose in the presence of adenosine-5' -triphosphate and magnesium ion, occupies an important position in the metabolism of sugars in both plants and animals. Humphreys and Garrard {kl) have presented evidence which suggests that the hexokinase reaction may be important in controlling the rate of glucose uptake by the com scutellumi an organ positioned between the root-shoot axis and endosperm of the com seed, where glucose absorbed from the endosperm is converted to sucrose which is subsequently translocated to the developing seedling during germination (28). Their data indicates that glucose-6-phosphate competitively inhibits an enzymatic step associated with net glucose uptake in scutelluia slices, and they suggest that the step might be the hexokinase-catalyzed phosphorylation of glucose. Since it has been demonstrated that brain hexokinase (15, I6) and to a small extent, yeast hexokinase (33), is inhibited by glucose-6-phosphate, although non competitively. It seemed desirable to investigate the properties of com scutellum hexokinase.

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