These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Catalytic subunit isoforms of mammalian lens Na,K-ATPase.
    Author: Garner MH, Horwitz J.
    Journal: Curr Eye Res; 1994 Jan; 13(1):65-77. PubMed ID: 8156827.
    Abstract:
    To identify the Na,K-ATPase isoforms present in the mammalian lens, seven antisera were prepared to selected peptide sequences of the catalytic (alpha) subunit. Three antisera were prepared to peptide sequences at the N-terminus of the three sequenced rat alpha isoforms. There is < 53% sequence homology among the isoforms in this region. Three antisera were prepared to peptide sequences at the ouabain binding site in the extracellular loop between membrane spanning sequences 1 and 2 of the sequenced rat alpha isoforms; sequence homology among the isoforms in this region is < 69%. An antiserum was also prepared to the carboxyl terminal region of the alpha 2 rat isoform. The sequenced isoforms (rat and human) in this region are > 94% homologous. The results from stains of Western blots of SDS-PAGE separations of lens membranes are presented. Alpha 1 is the predominant isoform of the epithelium. It is not found in cells of the central epithelium but is present in cells located more toward the equator. Alpha 3 is the catalytic subunit of the central 43% of the epithelium. The lens fiber cell membranes have a catalytic subunit that is related to the alpha 2 isoform. In the fiber cell a 98-100 kDa band stains with the antiserum to the alpha 2 N-terminus and the antiserum to the alpha 2 ouabain site. The antiserum to the alpha 2 C-terminus does not stain the 98-100 kDa band. (Preliminary reports of these results were presented at the 1992 and 1993 meetings of the Association for Research in Vision and Ophthalmology).
    [Abstract] [Full Text] [Related] [New Search]