Sequence analysis of βA3, βB3, and βA4 crystallins completes the identification of the major proteins in young human lens

Kirsten J. Lampi, Zhixiang Ma, Marjorie Shih, Thomas R. Shearer, Jean B. Smith, David L. Smith, Larry L. David

Research output: Contribution to journalArticle

163 Scopus citations

Abstract

A combination of Edman sequence analysis and mass spectrometry identified the major proteins of the young human lens as αA, αB, αA1, αA3, βA4, βB1, βB2, βB3, γS, γC, and γD-crystallins and mapped their positions on two-dimensional electrophoretic gels. The primary structures of human βA1, βA3, βA4, and βB3-crystallin subunits were predicted by determining cDNA sequences. Mass spectrometric analyses of each intact protein as well as the peptides from trypsin-digested proteins confirmed the predicted amino acid sequences and detected a partially degraded form of βA3/A1 missing either 22 or 4 amino acid residues from its N-terminal extension. These studies were a prerequisite for future studies to determine how human lens proteins are altered during aging and cataract formation.

Original languageEnglish (US)
Pages (from-to)2268-2275
Number of pages8
JournalJournal of Biological Chemistry
Volume272
Issue number4
DOIs
StatePublished - Jan 1 1997

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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