Immunoreactive forms of human erythrocyte ankyrin are present in diverse cells and tissues

No abstract is available for this paper.

• Publication year

  1979

• Venue

  Nature

• Publication date

  1979-10-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1038/281597a0PMID 492324
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes

  1979cited by this paper
• Identification by peptide analysis of the spectrin-binding protein in human erythrocytes.

  1979cited by this paper
• Identification and partial purification of ankyrin, the high affinity membrane attachment site for human erythrocyte spectrin.

  1979cited by this paper
• Syndeins: the spectrin-binding protein(s) of the human erythrocyte membrane.

  1979cited by this paper
• Purification of an active proteolytic fragment of the membrane attachment site for human erythrocyte spectrin.

  1978cited by this paper
• Spectrin is absent in various tissue culture cells

  1977cited by this paper
• Selective association of spectrin with the cytoplasmic surface of human erythrocyte plasma membranes. Quantitative determination with purified (32P)spectrin.

  1977cited by this paper
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  1999cites this paper
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  1995cites this paper
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  1994cites this paper
• Immunobiology of Proteins and Peptides VII

  1994cites this paper
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  1994cites this paper
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  1994cites this paper
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  1993cites this paper
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  1993cites this paper
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  1993cites this paper
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  1993cites this paper
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