Journal article
Yeast Hexokinase. I. Preparation of the Pure Enzyme
Biochemistry (Easton), Vol.5(12), pp.4003-4016
12/01/1966
DOI: 10.1021/bi00876a035
Abstract
A method is described for the preparation of baker's yeast hexokinase, which can be adapted for the preparation of yeast enzymes located at sites similar to that of hexokinase. It has been demonstrated by studies of the contaminating proteases that it is possible to isolate such an enzyme from yeast without apparent proteolytic degradation. This is achieved by rigorous maintenance of conditions ensuring the inhibition, including organophosphate inhibition, of the proteolytic enzymes. The procedure is then superior to previous hexokinase preparations in respect to the lack of degradation, the yield, the specific enzymic activity, the stability, and the preparation time. Two hexokinase species appear to be present under conditions of isolation, hexokinase A (in equal or larger amount) and hexokinase B. Each is a homogeneous protein by a number of criteria. Hexokinase B, as judged by criteria of homogeneity, purity, and stability, is a proteolytically undegraded enzyme having a specific activity of 800 units/mg at 25°; this is the highest reported for yeast hexokinase. Hexokinase A has a lower specific activity. Substrate specificity, chromatographic elution position, and electrophoretic mobility differences exist between these two species. © 1966, American Chemical Society. All rights reserved.
Details
- Title: Subtitle
- Yeast Hexokinase. I. Preparation of the Pure Enzyme
- Creators
- Norman R LazarusArmin H RamelYoucef M RustumEric A Barnard
- Resource Type
- Journal article
- Publication Details
- Biochemistry (Easton), Vol.5(12), pp.4003-4016
- Publisher
- American Chemical Society
- DOI
- 10.1021/bi00876a035
- ISSN
- 0006-2960
- eISSN
- 1520-4995
- Language
- English
- Date published
- 12/01/1966
- Academic Unit
- Hematology, Oncology, and Blood & Marrow Transplantation; Internal Medicine
- Record Identifier
- 9984359771702771
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