The induction of pyruvate kinase synthesis by heat shock inXenopus laevisembryos
作者:
M. Marsden,
R. W. Nickells,
M. Kapoor,
L. W. Browder,
期刊:
Developmental Genetics
(WILEY Available online 1993)
卷期:
Volume 14,
issue 1
页码: 51-57
ISSN:0192-253X
年代: 1993
DOI:10.1002/dvg.1020140107
出版商: Wiley Subscription Services, Inc., A Wiley Company
关键词: Xenopus;glycolysis;pyruvate kinase;heat shock protein
数据来源: WILEY
摘要:
AbstractHeat‐shockedXenopusembryos have an unusually complex heat shock response. The dominant heat shock protein (Hsp) has a relative molecular mass (Mr) of 62,000 D (Hsp62). Affinity‐purified IgGs against the glycolytic enzyme pyruvate kinase (PK; EC 2.7.1.40) specifically immunoprecipitated Hsp62 from extracts of embryos that had been heat‐shocked at 37°C for 30 min. Thus, Hsp62 and pyruvate kinase are immunologically cross‐reacting. Electrophoretic separation of PK isoforms suggests that heat‐shockedXenopusembryos increase synthesis of an isoform of PK. Thermal denaturation studies suggest that this isoform has enhanced thermal stability. The identification of PK as an Hsp is discussed within the context of a physiological requirement for elevated levels of anaerobic glycolysis in heatstressed cells as a vital component of the acquisition of thermotolerance. © 1993Wile
点击下载:
PDF
(688KB)
返 回