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Adenosinetriphosphate Cleavage During the G-Actin to F-Actin Transformation and the Binding of Adenosinetriphosphate to F-Actin

Description: Since the discovery of the Straub and Feuer as well as Laki et al. that ATP bound to G-actin is transformed to ADP and inorganic phosphate during polymerization of actin (1, 2), it has become increasingly clear that the chemical changes in the nucleotide are related to the change in the physical state of the protein. Barany, Biro, Molnar and Straub have shown that highly purified actin preparation free of any enzyme which would use ATP, ADP or AMP as a substrate still catalyze the breakdown of … more
Date: October 15, 1963
Creator: Barany, M.; Koshland, D. E., Jr.; Springhorn, S. S.; Finkleman, F. & Theratil-Anthony, T.
Item Type: Refine your search to only Report
Partner: UNT Libraries Government Documents Department
open access

Evidence for an Intermediate in Myosin Hydrolysis

Description: Ever since the hydrolysis of ATP by myosin was discovered the mechanism of this reaction has been a subject of intensive research. In some way the energy of the phosphate bond must be transferred to muscle protein so that chemical energy can be transformed into mechanical work. Formation of a phosphoryl-myosin intermediate has been suggested by many workers but evidence for such an intermediate has been elusive. ADP-32-ATP exchanges gave negative results and no P32-labeled myosin, other than th… more
Date: 1962
Creator: Koshland, Daniel E., Jr. & Levy, Harvey M.
Item Type: Refine your search to only Report
Partner: UNT Libraries Government Documents Department
open access

[News Script: Sports]

Description: Script from the WBAP-TV/NBC station in Fort Worth, Texas, relating a news story.
Date: July 1, 1969, 12:00 p.m.
Creator: WBAP-TV (Television station : Fort Worth, Tex.)
Item Type: Refine your search to only Script
Partner: UNT Libraries Special Collections
open access

Nucleotide Inhibition of Glyoxalase II

Description: The glyoxalase system mediates the conversion of methylglyoxal, a toxic ketoaldehyde, to D-lactic acid. The system is composed of two enzymes, glyoxalase I (Glo-I) and glyoxalase II (Glo-II), and exhibits an absolute requirement for a catalytic quantity of glutathione (GSH). Glo-I catalyzes the isomerization of a hemithioacetal, formed non-enzymatically from methylglyoxal and GSH, to the corresponding a -D-hydroxyacid thioester, s-D-lactoylglutathione (SLG). Glo-II catalyzes the irreversible br… more
Date: May 1999
Creator: Gillis, Glen S
Item Type: Refine your search to only Thesis or Dissertation
Partner: UNT Libraries
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