The modification of yeast hexokinases by proteases and its relationship to the dissociation of hexokinase into subunits.
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Summary
Crystalline hexokinase prepared by the method of Darrow and Colowick consists largely of enzyme which has been modified in its chromatographic and electrophoretic behavior by yeast protease which is present during the isolation procedure.
- Type
- article
- Published
- 1969-05-10
- Cited by
- 92
- References
- 0
- Access
- Open access
- OpenAlex
- https://openalex.org/W1584684324
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:28491147
Keywords
Hexokinase, Yeast, Proteases, Biochemistry, Chemistry
References
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- Structural proteins of adenoviruses. X. Isolation and topography of low molecular weight antigens from the virion of adenovirus type 2.
- Glucose exchange and catalysis by two crystalline hexokinase x glucose complexes. Evidence for an obligatory ATP-dependent conformational change in catalysis.
- The hexokinases: kinetic, physical, and regulatory properties.
- Chemical reactivity of the tyrosyl residues in yeast hexokinase. Properties of the nitroenzyme.
- Structure of yeast hexokinase. II. A 6 angstrom resolution electron density map showing molecular shape and heterologous interaction of subunits.
- Structure of yeast hexokinase. IV. Low-resoultion structure of enzyme-substrate complexes revealing negative co-operativity and allosteric interactions.
- Purification and crystallization of yeast hexokinase isoenzymes. Characterization of different forms by chromatofocusing.
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- Relaxation spectra of yeast hexokinases. Isomerization of the enzyme.
- Purine nucleoside diphosphate regulation of yeast hexokinases.
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