- n.
WordNet
- (chemistry, physics, biology) readily changed or destroyed by heat
English Journal
- Adaptive Evolution of Thermotoga maritima Reveals Plasticity of the ABC Transporter Network.
- Latif H1, Sahin M1, Tarasova J1, Tarasova Y1, Portnoy VA1, Nogales J1, Zengler K2.
- Applied and environmental microbiology.Appl Environ Microbiol.2015 Aug 15;81(16):5477-85. doi: 10.1128/AEM.01365-15. Epub 2015 Jun 5.
- Thermotoga maritima is a hyperthermophilic anaerobe that utilizes a vast network of ABC transporters to efficiently metabolize a variety of carbon sources to produce hydrogen. For unknown reasons, this organism does not metabolize glucose as readily as it does glucose di- and polysaccharides. The le
- PMID 26048924
- Acute rhabdomyolysis and inflammation.
- Hamel Y1, Mamoune A, Mauvais FX, Habarou F, Lallement L, Romero NB, Ottolenghi C, de Lonlay P.
- Journal of inherited metabolic disease.J Inherit Metab Dis.2015 Jul;38(4):621-8. doi: 10.1007/s10545-015-9827-7. Epub 2015 Mar 17.
- Rhabdomyolysis results from the rapid breakdown of skeletal muscle fibers, which leads to leakage of potentially toxic cellular content into the systemic circulation. Acquired causes by direct injury to the sarcolemma are most frequent. The inherited causes are: i) metabolic with failure of energy p
- PMID 25778939
- Interdomain hydrophobic interactions modulate the thermostability of microbial esterases from the hormone-sensitive lipase family.
- Li PY1, Chen XL1, Ji P1, Li CY1, Wang P1, Zhang Y1, Xie BB1, Qin QL1, Su HN1, Zhou BC1, Zhang YZ1, Zhang XY2.
- The Journal of biological chemistry.J Biol Chem.2015 Apr 24;290(17):11188-98. doi: 10.1074/jbc.M115.646182. Epub 2015 Mar 14.
- Microbial hormone-sensitive lipases (HSLs) contain a CAP domain and a catalytic domain. However, it remains unclear how the CAP domain interacts with the catalytic domain to maintain the stability of microbial HSLs. Here, we isolated an HSL esterase, E40, from a marine sedimental metagenomic library
- PMID 25771540
Japanese Journal
- Novel low-temperature-active, salt-tolerant and proteases-resistant endo-1,4-β-mannanase from a new Sphingomonas strain(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Zhou Junpei,Zhang Rui,Gao Yajie [他],Li Junjun,Tang Xianghua,Mu Yuelin,Wang Feng,Li Chao,Dong Yanyan,Huang Zunxi
- Journal of bioscience and bioengineering 113(5), 568-574, 2012-05
- … Purified rManAJB13 displayed the typical characteristics of low-temperature-active enzymes: showing apparent optimal at 40℃, 〜55% of the maximum activity at 20℃ and 〜20% at 10℃, and thermolability at 45℃ (〜15 mm half-life). …
- NAID 110009456893
- Biochemical Characterization of a Thermophilic Cellobiose 2-Epimerase from a Thermohalophilic Bacterium, Rhodothermus marinus JCM9785
- , , [他], , ,
- Bioscience, biotechnology, and biochemistry 75(11), 2162-2168, 2011-11-23
- … It efficiently produces epilactose carrying prebiotic properties from lactose, but the utilization of known CEs is limited due to thermolability. …
- NAID 10030396700
- Partial androgen insensitivity syndrome with thermolability in the androgen receptor
- HIRAOKA KENJI,KAWAUCHI AKIHIRO,SOH JINTETSU,OHE HIROSHI,SHIMA HIROKI,MIKI TSUNEHARU
- International journal of urology 13(1), 89-91, 2006-01-01
- NAID 10017244251
Related Links
- thermolability definition: adjective designating or of substances, as some toxins, enzymes, etc., that are destroyed or lose their characteristic properties when subjected to heat, esp. to a temperature of 55 C (131 F) or Login Menu ...
- thermolabile /ther·mo·la·bile/ (-la´bīl) easily affected by heat. ther·mo·la·bile (thûr′mō-lā′bĭl, -bīl′) adj. Subject to destruction ... In addition, to assess thermolability of the compounds, the plant extracts were boiled before addition to the ...
Related Pictures
★リンクテーブル★
| リンク元 | 「thermolabile」「熱不安定性」「heat-labile」「heat-unstable」「易熱性」 |
「thermolabile」
- adj.
- 易熱性の、熱不安定性の
「熱不安定性」
「heat-labile」
- 熱不安定性の
「heat-unstable」
- 熱不安定性の