Bovine lens 23, 21 and 19 kDa intrinsic membrane proteins have an identical amino-terminal amino acid sequence

Rao Gadiparthi, Karen A. Gutekunst, Robert L. Church

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

We have isolated bovine lens intrinsic membrane proteins (MP) having molecular masses of 19, 21 and 23 kDa. Limited amino acid sequence analysis of the amino-terminal portion of each of these polypeptides revealed a 100% homology in sequence for the number of residues determined (20 amino acids). Northern blot analysis of bovine lens mRNA using a labeled antisense oligonucleotide probe common to the amino acid sequence of these three peptides revealed a single band having an apparent molecular size of 0.8 kb. Taken together, these findings suggest a genetic commonality between these polypeptides.

Original languageEnglish (US)
Pages (from-to)483-486
Number of pages4
JournalFEBS Letters
Volume250
Issue number2
DOIs
StatePublished - Jul 3 1989

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Lenses
Amino Acid Sequence
Membrane Proteins
Amino Acids
Peptides
Oligonucleotide Probes
Antisense Oligonucleotides
Protein Sequence Analysis
Molecular mass
Sequence Homology
Northern Blotting
Messenger RNA

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Bovine lens 23, 21 and 19 kDa intrinsic membrane proteins have an identical amino-terminal amino acid sequence. / Gadiparthi, Rao; Gutekunst, Karen A.; Church, Robert L.

In: FEBS Letters, Vol. 250, No. 2, 03.07.1989, p. 483-486.

Research output: Contribution to journalArticle

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