Detail of > 338-69-2
- MSDS Download

- CAS Number:
- 338-69-2
- Name:
D-Alanine
- Formula:
- C3H7NO2
- Molecular Structure:

- Synonyms:
- D-alpha-Aminopropionsaeure;Ba 2776;D-alpha-alanine;(R)-2-Aminopropionsaeure;D-alpha-aminopropionic acid;D(-)-Alanine;H-D-Ala-OH;Alanine D-;D-Ala;D-Ala-OH;D-Alanine;D(-)-.alpha.-Alanine;(2R)-2-aminopropanoic acid;D-.alpha.-Alanine;Alanine, D-;(R)-2-aminopropanoic acid;D-Alanin;(R)-Alanine;D-2-Aminopropionic acid;Alanine D-form;D-(-)-Alanine;
- Molecular Weight:
- 89.09
- EINECS:
- 206-418-1
- Density:
- 1.161g/cm3
- Melting Point:
- 291 °C (dec.)(lit.)
- Boiling Point:
- 212.9 °C at 760 mmHg
- Flash Point:
- 82.6 °C
- Solubility:
- 155 g/L (20 °C) in water
- Appearance:
- White crystalline powder
- Hazard Symbols:
Xi- Risk Codes:
- 36/37/38
- Safety:
- 24/25-36-26Details
- particular:
- particular
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Reference
- Degradation of delta sleep inducing peptide (DSIP) and its analogs by brain extracts
- Degradation of delta sleep inducing peptide (DSIP) and its analogs by brain extracts. Marks, Neville; Stern, Frederic; Kastin, Abba J.; Coy, David H. (Res. Inst. Neurochem., Rockland Res. Inst., New York, N. Y., USA). Brain Res. Bull., 2(6), 491-3 (English) 1977. CODEN: BRBUDU. ISSN: 0361-9230. DOCUMENT TYPE: Journal CA Section: 6 (General Biochemistry) Section cross-reference(s): 13 Incubation of DSIP with an ext. of mouse brain resulted in release of tryptophan (indicating rapid action by a brain aminopeptidase) and release of serine (indicating internal cleavage by a brain neutral endopeptidase at the Ala6-Ser7 bond followed by the secondary action of an aminopeptidase). This mechanism was confirmed by detection of Gly8-Glu9 as a digest product. The finding of glutamate could be attributed to cleavage of this dipeptide or direct action of a carboxypeptidase on the nonapeptide. Other products that increased with time indicated secondary action of brain exopeptidase on peptide intermediates contg. the Gly-Gly subunit. Mechanisms of breakdown were confirmed by the use of DSIP analogs. D-Alanine in positions 3 and 4 blocked internal release of amino acids and peptides at short incubation periods but not the release of tryptophan. Addn. of tyrosine to position 1 failed to affect aminopeptidase and endopeptidase actions. The low yield of glutamate in the D-alanine analogs suggests that it was derived by secondary breakdown of Gly-Glu. Thus, the nonapeptide DSIP is a substrate for brain proteolytic enzymes and is degraded with release of N-terminal tryptophan along with other residues and peptide intermediates.
- Direct effect of luteinizing hormone-releasing hormone agonist on in vivo luteal progesterone secretion
- Direct effect of luteinizing hormone-releasing hormone agonist on in vivo luteal progesterone secretion. Macdonald, Gordan J.; Beattie, C. W.; Raj, H. G. M. (Dep. Anat., UMDNJ-Rutgers Med. Sch., Piscataway, NJ 08854, USA). Anterior Pituitary Gland, 319-25. Edited by: Bhatnagar, Ajay S. CNRS: Paris, Fr. (English) 1983. CODEN: 50SMAN. DOCUMENT TYPE: Conference CA Section: 2 (Mammalian Hormones) 6-D-Alanine-10-deglycinamide-LH-RH ethylamide [52435-06-0] induced pregnancy failure in hypophysectomized rats, an effect that was prevented by steroid replacement therapy. Therefore, the LH-RH analog is apparently capable of inhibiting ovarian steroidogenesis by an extrapituitary mechanism. In intact animals, any direct effect of LH-RH or LH-RH agonists on luteal progesterone [57-83-0] secretion would be accompanied by ovarian receptor down-regulation as a result of the LH-RH-induced excess of circulating LH.
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