Detail of > 407-41-0
- MSDS Download

- CAS Number:
- 407-41-0
- Name:
L-Serine, O-phosphono-
- Superlist Name:
- O-Phospho-L-serine
- Formula:
- C3H8NO6P
- Molecular Structure:

- Synonyms:
- L-Serine,dihydrogen phosphate (ester) (9CI);Serine phosphate, L- (6CI);Serine,dihydrogen phosphate (ester), L- (8CI);3-O-Phosphoserine;Dexfosfoserine;Fosforina;L-3-Phosphoserine;L-O-Phosphoserine;L-O-Serine phosphate;L-Phosphoserine;L-Serinephosphoric acid;L-Seryl phosphate;O-Phosphoryl-L-serine;O-Phosphorylserine;Phospho-L-serine;Serine O-phosphate;Serine dihydrogen phosphate (ester);
- Molecular Weight:
- 185.07
- EINECS:
- 206-986-0
- Density:
- 1.809 g/cm3
- Melting Point:
- 190 °C(lit.)
- Boiling Point:
- 475.4 °C at 760 mmHg
- Flash Point:
- 241.3 °C
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Reference
- 2-Amino-4-phosphonobutyrate selectively blocks mossy fiber-CA3 responses in guinea pig but not rat hippocampus
- 2-Amino-4-phosphonobutyrate selectively blocks mossy fiber-CA3 responses in guinea pig but not rat hippocampus. Lanthorn, Thomas H.; Ganong, Alan H.; Cotman, Carl W. (Dep. Psychobiol., Univ. California, Irvine, CA 92717, USA). Brain Res., 290(1), 174-8 (English) 1984. CODEN: BRREAP. ISSN: 0006-8993. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) Section cross-reference(s): 1 The acidic amino acid antagonist DL-2-amino-4-phosphonobutyrate (DL-APB) was a potent blocker of synaptic transmission at guinea pig, but not rat, mossy fiber-CA3 synapses in hippocampal slices. The L-isomer [23052-81-5] of APB was responsible for the potent inhibition at the guinea pig synapse. The L-APB analog L-serine-O-phosphate (L-SOP) [407-41-0] also was more potent against the guinea pig response. These differences may reflect a difference in a synaptic acidic amino acid receptor in these 2 species. Other acidic amino acid antagonists were less potent than APB or L-SOP and did not discriminate between the mossy fiber responses in the 2 species.
- Role of ionic environment in insolubilization of whey protein during heat treatment of whey products
- Role of ionic environment in insolubilization of whey protein during heat treatment of whey products. De Rham, O.; Chanton, S. (Res. Dep., Nestle Prod. Tech. Assist. Co. Ltd., La Tour de Peilz CH-1814, Switz.). J. Dairy Sci., 67(5), 939-49 (English) 1984. CODEN: JDSCAE. ISSN: 0022-0302. DOCUMENT TYPE: Journal CA Section: 17 (Food and Feed Chemistry) Proteins in whey were denatured by a heat treatment of 5 min at 95°. Near isoelec. pH, protein soly. dropped markedly but not at neutral pH unless the unmasked Ca concn. exceeded a threshold, itself pH dependent. Protein and lactose contents had little influence on insolubilization. Ca in whey was masked by citrate [77-92-9] and phosphate. Phosphoserine [407-41-0], phytate [83-86-3], and EDTA [60-00-4] also masked Ca. It was possible to obtain the same pH-insolubilization curve from whey and from demineralized whey mixed with whey ions (Ca 8 mM + Mg 3 mM + citrate 8 mM with or without phosphate 14 mM). Unmasked Ca was calcd. The unmasked Ca of whey protein conc. or dialyzed whey protein is highly dependent on conditions used in ultrafiltration or dialysis, and particularly on pH. The use of Rowland's noncasein N test for denatured whey protein measurement is only valid under restricted conditions. A model is proposed.
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