Table 2.
Identified sites of DHA and DHB on lens proteins.
| Protein: Peptide Residues | Modified Residue | Peptide with Modification |
|---|---|---|
| αA-crystallin: 118-145 | C131, C142 | YRLPSNVDQSALSC(ALK)SLSADGM(OX)LTFC(DHA)GPK |
|
αB-crystallin:
22-56 |
S35 | LFDQFFGEHLLES(DHA)DLFPTSTSLSPFYLRPPSFLR |
| αB-crystallin: 164-175 | T170 | EEKPAVT(DHB)AAPK |
| βA3-crystallin: 46-58 | C52 | M(OX)EFTSSC(DHA)PNVSERSFDNVR |
| βA3-crystallin: 65-95 | C82 | SLKVESGAWIGYEHTSFC(DHA)GQQFILERGEYPR |
| βA3-crystallin: 126-137 | T127 | M(OX)T(DHB)IFEKENFIGR |
| βA3-crystallin: 163-177 | C170 | IQSGAWVC(DHA)YQYPGYR |
|
βA4-crystallin:
2-7 |
C5 | T(ACE)LQC(DHA)TK |
| βA4-crystallin: 26-45 | C33 | RHEFTAEC(DHA)PSVLELGFETVR |
| βA4-crystallin: 159-177 | C166 | GFQYVLEC(DHA)DHHSGDYK |
| βB1-crystallin: 73-92 | C79 | RAEFSGEC(DHA)SNLADRGFDRVR |
| βB2-crystallin: 49-81 | C67 | AGSVLVQAGPWVGYEQANC(DHA)KGEQFVFEKGEYPR |
|
γB-crystallin:
16-32 |
C19, C23 | SYEC(DHA)TTDC(ALK)PNLQPYFSR |
|
γC-crystallin:
16-32 |
C23 | SLHVLEGC(DHA)WVLYELPNYR |
|
γD-crystallin:
16-38 |
C19 | HYEC(DHA)SSDHPNLQPYLSR |
| γD-crystallin: 102-117 | C109, C111 | EDYRGQMIEFTEDC(DHA)SC(ALK)LQDRFR |
|
γS-crystallin:
20-36 |
C23, C25, C27 | YDC(ALK)DC(ALK)DC(DHA)ADFHTYLSR |
|
BFSP1:
255-276 |
C259 | SAHEC(DHA)YDDEIQLYNEQIETLRK |
|
BFSP2:
53-72 |
C65 | APGVYVGTAPSGC(DHA)IGGLGAR |
|
BFSP2:
90-121 |
C114 | SSGLATVPAPGLERDHGAVEDLGGC(DHA)LVEYMAK |
|
BFSP2:
157-173 |
C161 | ASWASSC(DHA)QQVGEAVLENAR |
|
BFSP2:
251-276 |
C255 | QLAGC(DHA)ELEQMDAPIGTGLDDILETIR |
|
BFSP2:
318-339 |
C326 | VELHNTSC(DHA)QVQSLQAETESLR |
|
CBR1:
119-134 |
C122 | DVC(DHA)TELLPLIKPQGR |
*ALK refers to alkylated and a mass shift of 57.0215. OX refers to oxidized and a mass shift of 15.9949. ACE refers to acetylated and a mass shift of 42.0106. C(DHA) refers to a mass shift of -33.9877. S(DHA) and T(DHB) refer to a mass shift of -18.0106. BFSP1 and BFSP2 refer to filensin and phakinin, respectively.