Detail of > 1200-22-2
- MSDS Download

- CAS Number:
- 1200-22-2
- Name:
R-(+)-alpha-Lipoic acid
- Formula:
- C8H14O2S2
- Molecular Structure:

- Synonyms:
- 1,2-Dithiolane-3-pentanoicacid, (R)-;1,2-Dithiolane-3-valeric acid, (+)- (8CI);1,2-Dithiolane-3-pentanoicacid, (3R)-;(R)-Lipoic acid;(R)-a-Lipoic acid;Berlition;Byodinoral 300;Lipoec;Lipoic acid;R-(+)-Thioctic acid;Thioderm;Thiogamma;Tiobec;Tiobec Retard;d-Thioctic acid;a-(+)-Lipoic acid;a-Lipoic acid;
- Molecular Weight:
- 206.3256
- Density:
- 1.218 g/cm3
- Melting Point:
- 48-52 °C(lit.)
- Boiling Point:
- 362.5 °C at 760 mmHg
- Flash Point:
- 173 °C
- Appearance:
- yellow crystalline solid
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Reference
- Interactions of conjugated linoleic acid and lipoic acid on insulin action in the obese Zucker rat
- Interactions of conjugated linoleic acid and lipoic acid on insulin action in the obese Zucker rat. Teachey, Mary K.; Taylor, Zachary C.; Maier, Thomas; Saengsirisuwan, Vitoon; Sloniger, Julie A.; Jacob, Stephan; Klatt, Martin J.; Ptock, Arne; Kraemer, Klaus; Hasselwander, Oliver; Henriksen, Erik J. (Department of Physiology, Muscle Metabolism Laboratory, University of Arizona College of Medicine, GermanyTucson, AZ, USA). Metabolism, Clinical and Experimental, 52(9), 1167-1174 (English) 2003 W. B. Saunders Co. CODEN: METAAJ. ISSN: 0026-0495. DOCUMENT TYPE: Journal CA Section: 18 (Animal Nutrition) The fatty acid conjugated linoleic acid (CLA) and the antioxidant R-(+)-a-lipoic acid (R-ALA) individually enhance glucose tolerance and insulin action on skeletal muscle glucose transport in the insulin-resistant obese Zucker rat. To date, no study has assessed the potential interactions between these 2 interventions in treating insulin resistance. The present study was designed to det. whether chronic treatment with CLA and R-ALA in combination would enhance skeletal muscle glucose transport to a greater extent than either intervention individually. CLA, R-ALA, or a combination treatment of R-ALA and CLA were administered to female obese Zucker rats for 20 days at low or high doses. Whereas low-dose R-ALA (10 mg/kg body wt.Several substances with their cas registry numbers 1200-22-2 and 50-99-7 may be metioned in this study.) alone did not alter muscle glucose transport, low-dose CLA (0.3 g/kg) induced a significant increase (38%, P < .05) in insulin-mediated glucose transport in epitrochlearis, but not in soleus. Low-dose combination therapy brought about the greatest enhancement of insulin-mediated glucose transport in epitrochlearis (77%) and soleus (54%), with the latter effect being assocd. with a 50% redn. in protein carbonyls (an index of tissue oxidative stress) and a 33% diminution in muscle triglycerides. High-dose treatments with CLA (1.5 g/kg), R-ALA (50 mg/kg), and the combination of CLA and R-ALA elicited increases in insulin-mediated glucose transport in epitrochlearis (57%, 58%, and 77%) and soleus (32%, 35%, and 54%). However, whereas the individual high-dose treatments with CLA and R-ALA reduced protein carbonyls (63% and 49%) and triglycerides (29% and 28%) in soleus, no further redns. were obsd. with the high-dose combination treatment groups. These findings support a significant interaction between low doses of CLA and R-ALA for enhancement of insulin action on skeletal muscle glucose transport, possibly via redns. in muscle oxidative stress and in lipid storage. .
- Evidence for two protein-lipoylation activities in Escherichia coli
- Evidence for two protein-lipoylation activities in Escherichia coli. Brookfield, Dawn E.; Green, Jeffrey; Ali, Sohail T.; Machado, Rosane S.; Guest, John R.Chemicals with cas numbers 1200-22-2 and 4466-48-2 also play role. (Krebs Inst., Univ. Sheffield, Sheffield S10 2UH, UK). FEBS Lett., 295(1-3), 13-16 (English) 1991. CODEN: FEBLAL. ISSN: 0014-5793. DOCUMENT TYPE: Journal CA Section: 10 (Microbial, Algal, and Fungal Biochemistry) Section cross-reference(s): 7 The lipoate acyltransferase subunits of the 2-oxo acid dehydrogenase complexes are post-translationally modified with one or more covalently-bound lipoyl cofactors. Two distinct lipoate-protein ligase activities, LPL-A and LPL-B, have been detected in E. coli by their ability to modify purified lipoyl apo-domains of the bacterial pyruvate dehydrogenase complex. Both enzymes require ATP and Mg2+, use L-lipoate, 8-methylipoate, lipoyl adenylate and octanoyl adenylate as substrates, and both activate lipoyl-deficient pyruvate dehydrogenase complexes. In contrast, only LPL-B may be responsible uses D-lipoate and octanoate and there are differences in the metal-ion and phosphate requirements. It is suggested that LPL-B may be responsible for the octanoylation of lipoyl domains obsd. previously under lipoate-deficient conditions. .
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