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Detail of "980-21-2"

  • CAS Number:
  • 980-21-2
  • Name:
  • [1,1'-Biphenyl]-3,3'-dipropanoicacid, a3,a3'-diamino-6,6'-dihydroxy-

  • Molecular Structure:
  • Formula:
  • C18H20 N2 O6
  • Molecular Weight:
  • 0
  • Synonyms:
  • 3,3'-Biphenyldialanine,6,6'-dihydroxy- (6CI,7CI); 3,3'-Biphenyldipropionic acid, a,a'-diamino-6,6'-dihydroxy- (8CI);[1,1'-Biphenyl]-3,3'-dipropanoic acid, a,a'-diamino-6,6'-dihydroxy- (9CI); 3,3'-Bityrosine; 3,3'-Dityrosine;Bityrosine; Dityrosine; o,o-Dityrosine; o,o'-Dityrosine
  • Density:
  • 1.455g/cm3
  • Boiling Point:
  • 622.9°Cat760mmHg
  • Flash Point:
  • 330.5°C

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Reference

Covalent crosslinking and protein destruction induced by ozone
Covalent crosslinking and protein destruction induced by ozone. Ignatenko, A. V.; Cherenkevich, S. N. (Beloruss. State Univ., Minsk, USSR). Biofizika, 30(1), 18-22 (Russian) 1985. CODEN: BIOFAI. ISSN: 0006-3029. DOCUMENT TYPE: Journal CA Section: 4 (Toxicology) Section cross-reference(s): 6, 9 Spectroscopic method was used to monitor the O3-induced oxidn. of tyrosine [60-18-4] in proteins. The treatment caused crosslinking and degrdn. of proteins. Thus, O3 treatment of human serum albumins decreased the fluorescence intensity of the tyrosine components and caused appearance of a new band with max. at 320 nm. Analogous band was obsd. in the fluorescence spectrum of RNase [9001-99-4] after the reaction with O3. Correlation of the spectral properties of the band and that of 3,4-dihydroxyphenylalanine (3,4-DOPA) [59-92-7] indicates the formation of such a compd. in the proteins. Besides 3,4-DOPA, oxidized RNase showed a band at 411 nm (3,3-dityrosine [980-21-2]). Possible mechanisms of crosslinking by O3 are discussed.
Changes in collagens under the effects of oxidation agents
Changes in collagens under the effects of oxidation agents. Waykole, P.; Keller, C.; Heidemann, E. (Inst. Makromol. Chem., Tech. Hochsch. Darmstadt, Darmstadt, Ger.). Leder, 27(11), 190-7 (German) 1976. CODEN: LEDEA8. DOCUMENT TYPE: Journal CA Section: 41 (Leather and Related Materials) Dityrosine (I) [980-21-2] was formed by oxidn. of acid-sol. collagen by peracetic acid (II) [79-21-0] or Na2O2. I did not occur in the skin collagen of younger animals, but it was detected in the hide of an 18 yr-old cow. I was apparently an aging product and probably served to crosslink and stiffen the connective tissue. The oxidn. of collagen by II or Na2O2 caused a break between N- and C-atoms of the peptide chain as shown by the disintegration of the collagen peptides. The pyruvic acid [127-17-3] formed by splitting of alanine [56-41-7] was quant detd.
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