Detail of > 5466-22-8
- CAS Number:
- 5466-22-8
- Name:
Aminoacetonitrile sulfate
- Formula:
- 2(C2H4N2).H2SO4
- Molecular Structure:

- Synonyms:
- amino acetonitrile sulfate;Aminoacetonitrile sulfate 99%;Aminoacetonitrile (hydro)sulphate;bis[(cyanomethyl)ammonium] sulphate;cyanomethylazanium sulfate;Acetonitrile, amino-, sulfate (2:1) (8CI);Acetonitrile, amino-, sulfate (2:1);Bis((cyanomethyl)ammonium) sulphate;Aminoacetonitrile sulfate (2:1);Aminoacetonitril siran [Czech];
- Molecular Weight:
- 210.21
- EINECS:
- 226-772-0
- Melting Point:
- 160 °C (dec.)
- Boiling Point:
- 330 °C at 760 mmHg
- Flash Point:
- 264.5 °C
- Risk Codes:
- 24/25
- Safety:
- 36/37/39Details
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Reference
- Reversible decrease of collagen crosslinking by protein low diet and aminoacetonitrile
- Reversible decrease of collagen crosslinking by protein low diet and aminoacetonitrile. Effect of D-penicillamine and prednisolone on the rise of crosslinks. Ruiz-Torres, A.; Wille, G.; Robotta, R. (Inst. Inn. Med., Freie Univ. Berlin, Berlin, Ger.). Naunyn-Schmiedeberg's Arch. Pharmacol., 301(3), 241-4 (English) 1978. CODEN: NSAPCC. ISSN: 0369-5565. DOCUMENT TYPE: Journal CA Section: 3 (Biochemical Interactions) Section cross-reference(s): 1, 2 After ending a 4-wk period of low-protein diet with or without aminoacetonitrile sulfate [5466-22-8] the tail tendons of rats had an increase of hydroxylysinonorleucine (I) [66512-50-3] together with other unidentified reducible crosslinks. The binding of dihydroxylysinonorleucine type was an exception: its content remained unchanged. The rise in crosslinks after the 4-wk pretreatment with aminoacetonitrile was disturbed, when d-penicillamine [52-67-5] was given, because it specifically inhibited the formation of I. The content of other crosslink components was slightly increased above that of controls so that the abs. content of total isolated crosslinks increased in the presence of d-penicillamine. No differences were obtained with prednisolone Na 21-hemisuccinate [1715-33-9]. Apparently, aminoacetonitrile acts selectively on collagen crosslinking.
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