title: Expression of betaA2-crystallin in human lenses.
abstract: Evidence of betaA2-crystallin expression has been detected in human lenses. The protein, which co-elutes with betaA1/A3 from reversed phase HPLC separation of beta(L)-crystallins, accounts for 1-2% of the lens crystallins. Its molecular mass, M(r) 22 006, is consistent with the cDNA deduced sequence with addition of acetylation at the N-terminal serine residue. Approximately 20% of the protein is phosphorylated at Ser30.
authors.forename: Veniamin N
authors.initials: VN
authors.lastname: Lapko
authors.forename: David L
authors.initials: DL
authors.lastname: Smith
authors.forename: Jean B
authors.initials: JB
authors.lastname: Smith
mesh_terms: D000107:Acetylation; D000595:Amino Acid Sequence; D006801:Humans; D007908:Lens, Crystalline / Q000378:metabolism*; D013058:Mass Spectrometry / Q000379:methods; D010766:Phosphorylation; D038205:beta-Crystallin A Chain / Q000032:analysis*
chemical_list: D038205:beta-Crystallin A Chain