DBF (Disulfide Bond Forming) Enzyme from the Hyperthermophilic Archaebacterium Sulfolobus Solfataricus Behaves Like a Molecular Chaperone
DBF (Disulfide Bond Forming) Enzyme from the Hyperthermophilic Archaebacterium Sulfolobus Solfataricus Behaves Like a Molecular Chaperone
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来自超嗜热硫化叶古细菌 Solfataricus 的 DBF（二硫键形成）酶的行为类似于分子伴侣
DOI：
10.3109/10242429409034387
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发表时间：
1994
期刊：
影响因子：
2.9
通讯作者：
S. Bartolucci
中科院分区：
文献类型：
--
作者：
A. Guagliardi;L. Cerchia;L. Camardella;M. Rossi;S. Bartolucci
DBF enzyme from the hyperthermophilic archaebacterium Sulfolobus solfataricus greatly enhances the refolding at 30°C of denatured and reduced bovine pancreatic ribonuclease (Guagliardi et al., 1992). Here we show that DBF behaves like a molecular chaperone: it affects in an ATP-dependent manner the in vitro refolding at 50°C of two thermostable dehydrogenases, an alcohol dehydrogenase and a glutamate dehydrogenase from S. solfataricus. This paper also reports the complete amino acid sequence of DBF. The role of molecular chaperones from thermophilic microorganisms in applied biocatalysis is discussed.
影响因子：
2.9
作者：
S. Sadis;L. Hightower
通讯作者：
S. Sadis;L. Hightower